https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Maria+Matard-MannCAZypedia - User contributions [en-ca]2026-05-05T10:02:58ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=14137Carbohydrate Binding Module Family 162019-07-31T15:24:37Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|thumb|300px|right|'''Figure 1.''' The structure of CBM16-1 of ''Caldanaerobius polysaccharolyticus'' ManA, in complex with cellopentaose [{{PDBlink}}2zex PDB ID 2zex]. Four key residues of the binding cleft are highlighted. ]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate pentoses containing glucose and mannose, but only in the context of planar polymers like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as well as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite> (see Figure 1). <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified: Cloning of Man5A GH5 by Cann ''et al''. in 1999 reaveled the presence of two tandem CBM16 on the C-terminal end. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization: Bae ''et al''. solved in 2008 the first structures of the CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, [{{PDBlink}}2zew PDB ID 2zew], and two complexes of CBM16-1, one with cellopentaose [{{PDBlink}}2zex PDB ID 2zex] and one with mannopentaose [{{PDBlink}}2zey PDB ID 2zey]<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=14135Carbohydrate Binding Module Family 162019-07-31T15:23:42Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|thumb|300px|right|'''Figure 1.''' The structure of CBM16-1 of ''Caldanaerobius polysaccharolyticus'' ManA, in complex with cellopentaose [{{PDBlink}}2zex PDB ID 2zex]. Four key residues of the binding cleft are highlighted. ]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate pentoses containing glucose and mannose, but only in the context of planar polymers like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as well as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite> (see Figure 1). <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified: Cloning of Man5A GH5 by Cann ''et al''. in 1999 reaveled the presence of two tandem CBM16 on the C-terminal end. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization: Bae ''et al''. solved in 2008 the first structures of the CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, [{{PDBlink}}2zew PDB ID 2zew], 2zew <https://www.rcsb.org/structure/2zew>), and two complexes of CBM16-1, one with cellopentaose [{{PDBlink}}2zex PDB ID 2zex] and one with mannopentaose [{{PDBlink}}2zey PDB ID 2zey]<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=14088Carbohydrate Binding Module Family 162019-07-31T07:26:24Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|thumb|300px|right|'''Figure 1.''' The structure of CBM16-1 of ''Caldanaerobius polysaccharolyticus'' ManA, in complex with cellopentaose [PDBID: 2zex <https://www.rcsb.org/structure/2zex>]. Four key residues of the binding cleft are highlighted. ]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate pentoses containing glucose and mannose, but only in the context of planar polymers like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as well as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite> (see Figure 1). <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified: Cloning of Man5A GH5 by Cann ''et al''. in 1999 reaveled the presence of two tandem CBM16 on the C-terminal end. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization: Bae ''et al''. solved in 2008 the first structures of the CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, (PDBID: 2zew <https://www.rcsb.org/structure/2zew>, 2zez <https://www.rcsb.org/structure/2zez>), and two complexes of CBM16-1, one with cellopentaose (PDBID: 2zex <https://www.rcsb.org/structure/2zex>) and one with mannopentaose (PDBID: 2zey <https://www.rcsb.org/structure/2zey>)<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=14087Carbohydrate Binding Module Family 162019-07-31T07:24:33Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|thumb|300px|right|'''Figure 1.''' The structure of CBM16-1 of ''Caldanaerobius polysaccharolyticus'' ManA, in complex with cellopentaose. Four key residues of the binding cleft are highlighted. ]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate pentoses containing glucose and mannose, but only in the context of planar polymers like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as well as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite> (see Figure 1). <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified: Cloning of Man5A GH5 by Cann ''et al''. in 1999 reaveled the presence of two tandem CBM16 on the C-terminal end. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization: Bae ''et al''. solved in 2008 the first structures of the CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, (PDBID: 2zew <https://www.rcsb.org/structure/2zew>, 2zez <https://www.rcsb.org/structure/2zez>), and two complexes of CBM16-1, one with cellopentaose (PDBID: 2zex <https://www.rcsb.org/structure/2zex>) and one with mannopentaose (PDBID: 2zey <https://www.rcsb.org/structure/2zey>)<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=14086Carbohydrate Binding Module Family 162019-07-31T07:22:26Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|thumb|300px|right|'''Figure 1.''' The structure of CBM16-1 of ''Caldanaerobius polysaccharolyticus'' ManA, in complex with cellopentaose. Four key residues of the binding cleft are highlighted. ]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate pentoses containing glucose and mannose, but only in the context of planar polymers like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as well as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite> (see Figure 1). <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified: Cloning of Man5A GH5 by Cann ''et al''. in 1999 reaveled the presence of two tandem CBM16 on the C-terminal end. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization: Bae ''et al''. solved in 2008 the first structures of the CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, (PDBID: 2zew, 2zez), and two complexes of CBM16-1, one with cellopentaose (PDBID: [2zex <https://www.rcsb.org/structure/2zex>]) and one with mannopentaose (PDBID: 2zey)<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13626Carbohydrate Binding Module Family 162019-03-12T22:11:36Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|thumb|300px|right|'''Figure 1.''' The structure of CBM16-1 of ''Caldanaerobius polysaccharolyticus'' ManA, in complex with cellopentaose. Five key residues of the binding cleft are highlighted.]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate pentoses containing glucose and mannose, but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite> (see Figure 1). <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
Cloning of Man5A GH5 by Cann ''et al''. in 1999 reaveled the presence of two CBM16 tandem associated in C-terminal side. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization<br />
<br />
Bae ''et al''. solved in 2008 the first structures of CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, (PDBID: 2zew, 2zez), and two complexes of CBM16-1, one with cellopentaose (PDBID: 2zex) and one with mannopentaose (PDBID: 2zey)<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13625Carbohydrate Binding Module Family 162019-03-12T22:08:14Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|thumb|300px|right|'''Figure 1.''' The structure of CBM16-1 of ''Caldanaerobius polysaccharolyticus'' ManA, in complex with cellopentaose. Five key residues of the binding cleft are highlighted.]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate pentoses containing glucose and mannose, but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite> (see Figure 1). <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
Cloning of Man5A GH5 by Cann et al. in 1999 reaveled the presence of two CBM16 tandem associated in C-terminal side. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization<br />
<br />
Bae et al. solved in 2008 the first structures of CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, (PDBID: 2zew, 2zez), and two complexes of CBM16-1, one with cellopentaose (PDBID: 2zex) and one with mannopentaose (PDBID: 2zey)<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13624Carbohydrate Binding Module Family 162019-03-12T22:04:05Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|thumb|300px|right|'''Figure 1.''' The structure of CBM16-1 of ''Caldanaerobius polysaccharolyticus'' ManA, in complex with cellopentaose. Five key residues of the binding cleft are highlighted.]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (containing glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite> (see Figure 1). <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
Cloning of Man5A GH5 by Cann et al. in 1999 reaveled the presence of two CBM16 tandem associated in C-terminal side. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization<br />
<br />
Bae et al. solved in 2008 the first structures of CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, (PDBID: 2zew, 2zez), and two complexes of CBM16-1, one with cellopentaose (PDBID: 2zex) and one with mannopentaose (PDBID: 2zey)<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13623Carbohydrate Binding Module Family 162019-03-12T22:01:12Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|thumb|300px|right|'''Figure 1.''' The structure of CBM16-1 of ''Caldanaerobius polysaccharolyticus'' ManA, in complex with cellopentaose. PDBID: 2zex]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (containing glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite>. <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
Cloning of Man5A GH5 by Cann et al. in 1999 reaveled the presence of two CBM16 tandem associated in C-terminal side. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization<br />
<br />
Bae et al. solved in 2008 the first structures of CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, (PDBID: 2zew, 2zez), and two complexes of CBM16-1, one with cellopentaose (PDBID: 2zex) and one with mannopentaose (PDBID: 2zey)<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13622Carbohydrate Binding Module Family 162019-03-12T21:58:00Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|thumb|300px|right|'''Figure 1.''' The structure of CBM16-1 of ''Caldanaerobius polysaccharolyticus'' ManA]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (containing glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite>. <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
Cloning of Man5A GH5 by Cann et al. in 1999 reaveled the presence of two CBM16 tandem associated in C-terminal side. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization<br />
<br />
Bae et al. solved in 2008 the first structures of CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, (PDBID: 2zew, 2zez), and two complexes of CBM16-1, one with cellopentaose (PDBID: 2zex) and one with mannopentaose (PDBID: 2zey)<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13536Carbohydrate Binding Module Family 162019-02-08T18:27:41Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|200px|right]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (containing glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite>. <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
Cloning of Man5A GH5 by Cann et al. in 1999 reaveled the presence of two CBM16 tandem associated in C-terminal side. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization<br />
<br />
Bae et al. solved in 2008 the first structures of CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, (PDBID: 2zew, 2zez), and two complexes of CBM16-1, one with cellopentaose (PDBID: 2zex) and one with mannopentaose (PDBID: 2zey)<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13535Carbohydrate Binding Module Family 162019-02-08T18:26:11Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|200px|right]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (containing glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite>. <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
Cloning of Man5A GH5 by Cann et al. in 1999 reaveled the presence of two CBM16 tandem associated in C-terminal side. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization<br />
<br />
Bae et al. solved the first structures of CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, (PDBID: 2zew, 2zez), and two complexes of CBM16-1, one with cellopentaose (PDBID: 2zex) and one with mannopentaose (PDBID: 2zey)<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13534Carbohydrate Binding Module Family 162019-02-08T18:23:22Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|200px|right]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (containing glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite>. <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
Cloning of Man5A GH5 by Cann et al. in 1999 reaveled the presence of two CBM16 tandem associated in C-terminal side. Their deletion resulted in failure of the catalytic module to bind to cellulose column, and significant loss of both mannanase and carboxy methylcellulase activities <cite>Cann1999</cite>.<br />
<br />
;First Structural Characterization<br />
<br />
Bae et al. solved the first structures of CBM16 family: both modules of ''Caldanaerobius polysaccharolyticus'' Man5A, (PDBID: 2zew, 2zez), and two complexes of CBM16-1, one with cellopentaose (PDBID: 2zex) and one with mannopentaose (PDBID: 2zey)<cite>Bae2008</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
#Barbeyron1998 pmid=9580981<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=19270083<br />
#Dong2014 pmid=25210041<br />
#Sim2017 pmid=29057942<br />
<br />
#Sunna2001 pmid=11389686<br />
#Cann1999 pmid=10049399<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13533Carbohydrate Binding Module Family 162019-02-08T17:58:11Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2018</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2018</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2018</cite>.<br />
<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|200px|right]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (containing glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite>. <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
<cite>Cann1999</cite>: two CBM16 tandem associated, in C-terminal side of the Man5A GH5<br />
;First Structural Characterization<br />
<cite>Bae2008</cite><br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=18025086<br />
#Su2010 pmid=20739280<br />
<br />
#Barbeyron1998 pmid=<br />
<br />
#Matard-Mann2017 pmid=29030427<br />
#Salmean2018 pmid=29410423<br />
#Barabote2009 pmid=<br />
<br />
#Dong2014 pmid=<br />
#Sim2017 pmid=<br />
<br />
#Sunna2001 pmid=<br />
<br />
#Cann1999 pmid=<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13532Carbohydrate Binding Module Family 162019-02-08T17:49:42Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2017</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2017</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2017</cite>.<br />
<br />
<br />
== Structural Features ==<br />
[[File:CBM16-1.png|200px|right]]<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (containing glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite>. <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
<cite>Cann1999</cite>: two CBM16 tandem associated, in C-terminal side of the Man5A GH5<br />
;First Structural Characterization<br />
<cite>Bae2008</cite><br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=<br />
#Su2010 pmid=<br />
#Barbeyron1998 pmid=<br />
#Matard-Mann2017 pmid=<br />
#Salmean2017 pmid=<br />
<br />
#Barabote2009 pmid=<br />
<br />
#Dong2014 pmid=<br />
#Sim2017 pmid=<br />
<br />
#Sunna2001 pmid=<br />
<br />
#Cann1999 pmid=<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=File:CBM16-1.png&diff=13531File:CBM16-1.png2019-02-08T17:48:07Z<p>Maria Matard-Mann: Maria Matard-Mann uploaded a new version of File:CBM16-1.png</p>
<hr />
<div>PDB file 2ZEX</div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13530Carbohydrate Binding Module Family 162019-02-08T17:32:37Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
[[File:CBM16-1.png|200px|right]]<br />
== Ligand specificities ==<br />
Family 16 CBMs ([http://www.cazy.org/CBM16.html CAZy - CBM16]) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: [[GH5]] mannanases <cite>Bae2008 Su2010</cite>, [[GH16]] kappa carrageenases <cite>Barbeyron1998 Matard-Mann2017 Salmean2017</cite>, [[GH18]] chitinases <cite>Barabote2009</cite> and [[PL18]] alginate lyases <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated <cite>Bae2008 Su2010 Salmean2017</cite>. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays <cite>Salmean2017</cite>.<br />
<br />
<br />
== Structural Features ==<br />
<br />
CBM16 is a [[Carbohydrate-binding_modules#Types|type B]] CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (containing glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBMs from ''Caldanaerobius polysaccharolyticus'' (formerly ''Thermoanaerobacterium polysaccharolyticum'') ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite>. <br />
<br />
Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the [[CBM4]], [[CBM17]], [[CBM22]] and [[CBM27]] families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
<cite>Cann1999</cite>: two CBM16 tandem associated, in C-terminal side of the Man5A GH5<br />
;First Structural Characterization<br />
<cite>Bae2008</cite><br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=<br />
#Su2010 pmid=<br />
#Barbeyron1998 pmid=<br />
#Matard-Mann2017 pmid=<br />
#Salmean2017 pmid=<br />
<br />
#Barabote2009 pmid=<br />
<br />
#Dong2014 pmid=<br />
#Sim2017 pmid=<br />
<br />
#Sunna2001 pmid=<br />
<br />
#Cann1999 pmid=<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=File:CBM16-1.png&diff=13529File:CBM16-1.png2019-02-08T17:30:08Z<p>Maria Matard-Mann: PDB file 2ZEX</p>
<hr />
<div>PDB file 2ZEX</div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=User:Maria_Matard-Mann&diff=13528User:Maria Matard-Mann2019-02-08T17:26:42Z<p>Maria Matard-Mann: </p>
<hr />
<div>[[Image:Algascience.png|200px|right]]<br />
<br />
Maria Matard-Mann obtained her B.Sc. in Biology from the University of Rennes and completed her PhD in 2017 under the supervision of ^^^Mirjam Czjzek^^^ at the University of Pierre et Marie Curie (Sorbonne, Paris). The work focused on biochemical and structural studies of glycoside hydrolases from families [[GH16]], [[GH29]] and a non classified family related to [[GH42]]. She is currently working as research project manager for the company Olmix. She has determined the crystal structures of<br />
<br />
* [[GH16]] ''Zobellia galactanivorans'' kappa-carrageenase [ [[User:Maria Matard#bibkey_Matard-Mann2017|1]] ]<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Matard-Mann2017 pmid=29030427<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Matard-Mann,Maria]]<br />
<!-- ATTENTION: Make sure to replace "Lastname,Firstname" with your own name, for proper sorting of the Contributors page. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=File:Algascience.png&diff=13527File:Algascience.png2019-02-08T17:23:03Z<p>Maria Matard-Mann: Maria Matard-Mann uploaded a new version of File:Algascience.png</p>
<hr />
<div></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=File:Algascience.png&diff=13526File:Algascience.png2019-02-08T17:17:11Z<p>Maria Matard-Mann: </p>
<hr />
<div></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13494Carbohydrate Binding Module Family 162019-02-01T10:35:48Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs are found essentially in bacteria (only 4 are in archaea compared to 494 bacteria inventoried in CAZY). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: GH5 mannanase <cite>Bae2008 Su2010</cite>, GH16 kappa carrageenase <cite>Barbeyron1998 Matard-Mann2017 Salmean2017</cite>, GH18 chitinase <cite>Barabote2009</cite> and PL18 alginate lyase <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC analysis and crystallography of complex with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach on polysaccharide microarray <cite>Salmean2017</cite>.<br />
<br />
<br />
== Structural Features ==<br />
<br />
CBM16 is a type B CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBM of Caldanaerobius polysaccharolyticus (formerly Thermoanaerobacterium polysaccharolyticum) ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Study of affinity of targeted mutant for the predicted key resides confirmed the importance of two tryptophanes (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite>.<br />
<br />
Based on sequence similarity and conservation of secondary structure element, it has been proposed that along with the CBM-4, 17, 22 and 27 families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of Caldanaerobius polysaccharolyticus, the deletion of its both CBM16 severely impaired the ability of the catalytic module (GH5) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from Zobellia galactanivorans, the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module (GH16) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family PL18, it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperon function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
<cite>Cann1999</cite>: two CBM16 tandem associated, in C-terminal side of the Man5A GH5<br />
;First Structural Characterization<br />
<cite>Bae2008</cite><br />
<br />
== References ==<br />
<biblio><br />
#Bae2008 pmid=<br />
#Su2010 pmid=<br />
#Barbeyron1998 pmid=<br />
#Matard-Mann2017 pmid=<br />
#Salmean2017 pmid=<br />
<br />
#Barabote2009 pmid=<br />
<br />
#Dong2014 pmid=<br />
#Sim2017 pmid=<br />
<br />
#Sunna2001 pmid=<br />
<br />
#Cann1999 pmid=<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13493Carbohydrate Binding Module Family 162019-02-01T10:29:05Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs are found essentially in bacteria (only 4 are in archaea compared to 494 bacteria inventoried in CAZY). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: GH5 mannanase <cite>Bae2008 Su2010</cite>, GH16 kappa carrageenase <cite>Barbeyron1998 Matard-Mann2017 Salmean2017</cite>, GH18 chitinase <cite>Barabote2009</cite> and PL18 alginate lyase <cite>Dong2014 Sim2017</cite>. Binding to glucomannan and kappa-carrageenan has been demonstrated. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC analysis and crystallography of complex with pentomannan and pentoglucan <cite>Bae2008 Su2010</cite>. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach on polysaccharide microarray <cite>Salmean2017</cite>.<br />
<br />
<br />
== Structural Features ==<br />
<br />
CBM16 is a type B CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans <cite>Bae2008</cite>. The crystallographic structure determination of both CBM of Caldanaerobius polysaccharolyticus (formerly Thermoanaerobacterium polysaccharolyticum) ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft <cite>Bae2008</cite>. Study of affinity of targeted mutant for the predicted key resides confirmed the importance of two tryptophanes (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) <cite>Su2010</cite>.<br />
<br />
Based on sequence similarity and conservation of secondary structure element, it has been proposed that along with the CBM-4, 17, 22 and 27 families, they form a superfamily <cite>Sunna2001</cite>.<br />
<br />
<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of Caldanaerobius polysaccharolyticus, the deletion of its both CBM16 severely impaired the ability of the catalytic module (GH5) to bind cellulose <cite>Cann1999</cite>.<br />
<br />
In the case of CgkA from Zobellia galactanivorans, the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module (GH16) <cite>Matard-Mann2017</cite>.<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family PL18, it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperon function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.<br />
<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
<cite>Cann 1999</cite>: two CBM16 tandem associated, in C-terminal side of the Man5A GH5<br />
;First Structural Characterization<br />
<cite>Bae 2008</cite><br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].<br />
#Boraston2004 pmid=15214846<br />
#Hashimoto2006 pmid=17131061<br />
#Shoseyov2006 pmid=16760304<br />
#Guillen2010 pmid=19908036<br />
#Armenta2017 pmid=28547780<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13492Carbohydrate Binding Module Family 162019-02-01T10:21:00Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs are found essentially in bacteria (only 4 are in archaea compared to 494 bacteria inventoried in CAZY). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: GH5 mannanase (<cite>Bae 2008, Su 2010</cite>), GH16 kappa carrageenase (<cite>Barbeyron 1998, Matard-Mann 2017, Salmean 2017</cite>), GH18 chitinase (<cite>Barabote 2009</cite>) and PL18 alginate lyase (<cite>Dong, 2014; Sim 2017</cite>). Binding to glucomannan and kappa-carrageenan has been demonstrated. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC analysis and crystallography of complex with pentomannan and pentoglucan (<cite>Bae et al., 2008; Su 2010</cite>). Conversely, binding to kappa-carrageenan has been shown by a double-blind approach on polysaccharide microarray (<cite>Salmean 2017</cite>).<br />
<br />
<br />
== Structural Features ==<br />
<br />
CBM16 is a type B CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans (<cite>Bae 2008</cite>). The crystallographic structure determination of both CBM of Caldanaerobius polysaccharolyticus (formerly Thermoanaerobacterium polysaccharolyticum) ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft (<cite>Bae 2008</cite>). Study of affinity of targeted mutant for the predicted key resides confirmed the importance of two tryptophanes (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) (<cite>Su 2010</cite>).<br />
<br />
Based on sequence similarity and conservation of secondary structure element, it has been proposed that along with the CBM-4, 17, 22 and 27 families, they form a superfamily (<cite>Sunna, 2001).<br />
<br />
<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of Caldanaerobius polysaccharolyticus, the deletion of its both CBM16 severely impaired the ability of the catalytic module (GH5) to bind cellulose (<cite>Cann 1999</cite>).<br />
<br />
In the case of CgkA from Zobellia galactanivorans, the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module (GH16) (<cite>Matard-Mann 2017</cite>).<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family PL18, it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now (<cite>Sim 2017</cite>). A chaperon function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module (<cite>Dong 2014</cite>).<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
<cite>Cann 1999</cite>: two CBM16 tandem associated, in C-terminal side of the Man5A GH5<br />
;First Structural Characterization<br />
<cite>Bae 2008</cite><br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].<br />
#Boraston2004 pmid=15214846<br />
#Hashimoto2006 pmid=17131061<br />
#Shoseyov2006 pmid=16760304<br />
#Guillen2010 pmid=19908036<br />
#Armenta2017 pmid=28547780<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_16&diff=13491Carbohydrate Binding Module Family 162019-02-01T10:14:22Z<p>Maria Matard-Mann: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: [[User:Maria_Matard-Mann|Maria Matard-Mann]]<br />
* [[Responsible Curator]]: ^^^Elizabeth Ficko-Blean^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM16.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Family 16 CBMs are found essentially in bacteria (only 4 are in archaea compared to 494 bacteria inventoried in CAZY). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: GH5 mannanase (Bae 2008, Su 2010), GH16 kappa carrageenase (Barbeyron 1998, Matard-Mann 2017, Salmean 2017), GH18 chitinase (Barabote 2009) and PL18 alginate lyase (Dong, 2014; Sim 2017). Binding to glucomannan and kappa-carrageenan has been demonstrated. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC analysis and crystallography of complex with pentomannan and pentoglucan (Bae et al., 2008; Su 2010 ). Conversely, binding to kappa-carrageenan has been shown by a double-blind approach on polysaccharide microarray (Salmean 2017).<br />
<br />
Mention here all major natural ligand specificities that are found within a given family (also plant or mammalian origin). Certain linkages and promiscuity would also be mentioned here if biologically relevant.<br />
''Note: Here is an example of how to insert references in the text, together with the "biblio" section below:'' Please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. CBMs, in particular, have been extensively reviewed <cite>Boraston2004 Hashimoto2006 Shoseyov2006 Guillen2010 Armenta2017</cite>.<br />
<br />
== Structural Features ==<br />
<br />
CBM16 is a type B CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans (Bae 2008). The crystallographic structure determination of both CBM of Caldanaerobius polysaccharolyticus (formerly Thermoanaerobacterium polysaccharolyticum) ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft (Bae 2008). Study of affinity of targeted mutant for the predicted key resides confirmed the importance of two tryptophanes (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) (Su 2010).<br />
<br />
Based on sequence similarity and conservation of secondary structure element, it has been proposed that along with the CBM-4, 17, 22 and 27 families, they form a superfamily (Sunna, 2001).<br />
<br />
<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)<br />
* '''Type:''' Include here Type A, B, or C and properties<br />
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.<br />
<br />
== Functionalities ==<br />
<br />
In the Man5A of Caldanaerobius polysaccharolyticus, the deletion of its both CBM16 severely impaired the ability of the catalytic module (GH5) to bind cellulose (Cann 1999).<br />
<br />
In the case of CgkA from Zobellia galactanivorans, the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module (GH16) (Matard-Mann 2017).<br />
<br />
Even if frequently found within the gene coding for alginate lyase from family PL18, it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now (Sim 2017). A chaperon function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module (Dong 2014).<br />
''Content in this section should include, in paragraph form, a description of:''<br />
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.<br />
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)<br />
* '''Novel Applications:''' Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
Cann 1999: two CBM16 tandem associated, in C-terminal side of the Man5A GH5<br />
;First Structural Characterization<br />
Bae 2008<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].<br />
#Boraston2004 pmid=15214846<br />
#Hashimoto2006 pmid=17131061<br />
#Shoseyov2006 pmid=16760304<br />
#Guillen2010 pmid=19908036<br />
#Armenta2017 pmid=28547780<br />
</biblio><br />
<br />
[[Category:Carbohydrate Binding Module Families|CBM016]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=User:Maria_Matard-Mann&diff=13095User:Maria Matard-Mann2018-06-04T08:22:06Z<p>Maria Matard-Mann: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
<br />
Maria Matard-Mann obtained her B.Sc. in Biology from the University of Rennes and completed her PhD in 2017 under the supervision of Mirjam Czjzek at the University of Pierre et Marie Curie (Sorbonne, Paris). The work focused on biochemical and structural studies of glycoside hydrolases from families GH16, GH29 and a non classified family related to GH42. She is currently working as research project manager for the company Olmix. She has determined the crystal structures of<br />
<br />
* [[GH16]] ''Zobellia galactanivorans'' kappa-carrageenase [ [[User:Maria Matard#bibkey_Matard-Mann2017|1]] ]<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Matard-Mann2017 pmid=29030427<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Matard-Mann,Maria]]<br />
<!-- ATTENTION: Make sure to replace "Lastname,Firstname" with your own name, for proper sorting of the Contributors page. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=User:Maria_Matard-Mann&diff=13094User:Maria Matard-Mann2018-06-04T08:21:34Z<p>Maria Matard-Mann: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
<br />
Maria Matard-Mann obtained her B.Sc. in Biology from the University of Rennes and completed her PhD in 2017 under the supervision of Mirjam Czjzek at the University of Pierre et Marie Curie (Sorbonne, Paris). The work focused on biochemical and structural studies of glycoside hydrolases from families GH16, GH29 and a non classified family related to GH42. She is currently working as research project manager for the company Olmix. She has determined the crystal structures of<br />
<br />
[[GH16]] ''Zobellia galactanivorans'' kappa-carrageenase [ [[User:Maria Matard#bibkey_Matard-Mann2017|1]] ]<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Matard-Mann2017 pmid=29030427<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Matard-Mann,Maria]]<br />
<!-- ATTENTION: Make sure to replace "Lastname,Firstname" with your own name, for proper sorting of the Contributors page. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=User:Maria_Matard-Mann&diff=13093User:Maria Matard-Mann2018-06-04T08:21:01Z<p>Maria Matard-Mann: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
<br />
Maria Matard-Mann obtained her B.Sc. in Biology from the University of Rennes and completed her PhD in 2017 under the supervision of Mirjam Czjzek at the University of Pierre et Marie Curie (Sorbonne, Paris). The work focused on biochemical and structural studies of glycoside hydrolases from families GH16, GH29 and a non classified family related to GH42. She is currently working as research project manager for the company Olmix. She has determined the crystal structures of<br />
<br />
[[GH16]] ''Zobellia galactanivorans'' kappa-carrageenase [[[User:Maria Matard#bibkey_Matard-Mann2017|1]]]<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Matard-Mann2017 pmid=29030427<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Matard-Mann,Maria]]<br />
<!-- ATTENTION: Make sure to replace "Lastname,Firstname" with your own name, for proper sorting of the Contributors page. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=User:Maria_Matard-Mann&diff=13092User:Maria Matard-Mann2018-06-04T08:19:11Z<p>Maria Matard-Mann: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
<br />
Maria Matard-Mann obtained her B.Sc. in Biology from the University of Rennes and completed her PhD in 2017 under the supervision of Mirjam Czjzek at the University of Pierre et Marie Curie (Sorbonne, Paris). The work focused on biochemical and structural studies of glycoside hydrolases from families GH16, GH29 and a non classified family related to GH42. She is currently working as research project manager for the company Olmix. She has determined the crystal structures of<br />
<br />
[[GH16]] ''Zobellia galactanivorans'' kappa-carrageenase [[User:Maria Matard#bibkey_Matard-Mann2017|1]]<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Matard-Mann2017 pmid=29030427<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Matard-Mann,Maria]]<br />
<!-- ATTENTION: Make sure to replace "Lastname,Firstname" with your own name, for proper sorting of the Contributors page. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=User:Maria_Matard-Mann&diff=13091User:Maria Matard-Mann2018-06-04T08:18:52Z<p>Maria Matard-Mann: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
<br />
Maria Matard-Mann obtained her B.Sc. in Biology from the University of Rennes and completed her PhD in 2017 under the supervision of Mirjam Czjzek at the University of Pierre et Marie Curie (Sorbonne, Paris). The work focused on biochemical and structural studies of glycoside hydrolases from families GH16, GH29 and a non classified family related to GH42. She is currently working as research project manager for the company Olmix. She has determined the crystal structures of<br />
<br />
[[GH16]] ''Zobellia galactanivorans'' kappa-carrageenase [[[User:Maria Matard#bibkey_Matard-Mann2017|1]]]<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Matard-Mann2017 pmid=29030427<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Matard-Mann,Maria]]<br />
<!-- ATTENTION: Make sure to replace "Lastname,Firstname" with your own name, for proper sorting of the Contributors page. --></div>Maria Matard-Mannhttps://www.cazypedia.org/index.php?title=User:Maria_Matard-Mann&diff=13090User:Maria Matard-Mann2018-06-04T08:18:18Z<p>Maria Matard-Mann: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
'''This is an empty template to help you get started with composing your User page.'''<br />
Maria Matard-Mann obtained her B.Sc. in Biology from the University of Rennes and completed her PhD in 2017 under the supervision of Mirjam Czjzek at the University of Pierre et Marie Curie (Sorbonne, Paris). The work focused on biochemical and structural studies of glycoside hydrolases from families GH16, GH29 and a non classified family related to GH42. She is currently working as research project manager for the company Olmix. She has determined the crystal structures of<br />
<br />
[[GH16]] ''Zobellia galactanivorans'' kappa-carrageenase [[[User:Maria Matard#bibkey_Matard-Mann2017|1]]]<br />
<br />
<br />
<br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Matard-Mann2017 pmid=29030427<br />
<br />
</biblio><br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Matard-Mann,Maria]]<br />
<!-- ATTENTION: Make sure to replace "Lastname,Firstname" with your own name, for proper sorting of the Contributors page. --></div>Maria Matard-Mann