Carbohydrate Binding Module Family 73 - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:14:00Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Elizabeth Ficko-Blean: /* Ligand specificities */

2018-10-11T14:45:26Z

Ligand specificities

Elizabeth Ficko-Blean at 14:27, 11 October 2018

2018-10-11T14:27:05Z

Elizabeth Ficko-Blean at 09:59, 28 September 2018

2018-09-28T09:59:12Z

Gustav Vaaje-Kolstad at 11:18, 25 September 2018

2018-09-25T11:18:26Z

Gustav Vaaje-Kolstad at 11:16, 25 September 2018

2018-09-25T11:16:59Z

Gustav Vaaje-Kolstad at 11:10, 25 September 2018

2018-09-25T11:10:17Z

Gustav Vaaje-Kolstad at 11:05, 25 September 2018

2018-09-25T11:05:47Z

Gustav Vaaje-Kolstad at 07:43, 25 September 2018

2018-09-25T07:43:28Z

Elizabeth Ficko-Blean at 09:45, 21 September 2018

2018-09-21T09:45:59Z

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
 {{CuratorApproved}}
-* [[Author]]: ^^^Zarah Forsberg^^^
+* [[Author]]: [[User:Zarah Forsberg|Zarah Forsberg]]
-* [[Responsible Curator]]:  ^^^Gustav Vaaje-Kolstad^^^
+* [[Responsible Curator]]:  [[User:Gustav Vaaje-Kolstad|Gustav Vaaje-Kolstad]]
 ----

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 == Ligand specificities ==
-Family 73 CBMs are modules of approximately 60 residues that are appended to bacterial enzymes associated to chitin degradation <cite>Forsberg2016 Wong2012 Tuveng2016</cite>. Binding to amorphous and crystalline α- and β-chitin has been demonstrated <cite>Forsberg2016 Wong2012</cite>. The CBM73 module of the tri-modular LPMO, ''Cj''LPMO10A, binds tightly to α- chitin (Kd = 4.3 µM) and binding equilibrium is established within 15 minutes after mixing the protein and substrate  <cite>Forsberg2016</cite>.
+Family 73 CBMs are modules of approximately 60 residues that are appended to bacterial enzymes associated to chitin degradation <cite>Forsberg2016 Wong2012 Tuveng2016</cite>. Binding to amorphous and crystalline α- and β-chitin has been demonstrated <cite>Forsberg2016 Wong2012</cite>. The CBM73 module of the tri-modular LPMO, ''Cj''LPMO10A, binds tightly to α- chitin (Kd = 4.3 µM) and binding equilibrium was established within 15 minutes after mixing the protein and ligand  <cite>Forsberg2016</cite>.
 == Structural Features ==

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
-{{UnderConstruction}}
+{{CuratorApproved}}
 * [[Author]]: ^^^Zarah Forsberg^^^
 * [[Responsible Curator]]:  ^^^Gustav Vaaje-Kolstad^^^

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 == Ligand specificities ==
 Family 73 CBMs are modules of approximately 60 residues that are appended to bacterial enzymes associated to chitin degradation <cite>Forsberg2016 Wong2012 Tuveng2016</cite>. Binding to amorphous and crystalline α- and β-chitin has been demonstrated <cite>Forsberg2016 Wong2012</cite>. The CBM73 module of the tri-modular LPMO, ''Cj''LPMO10A, binds tightly to α- chitin (Kd = 4.3 µM) and binding equilibrium is established within 15 minutes after mixing the protein and substrate  <cite>Forsberg2016</cite>.
 == Structural Features ==

← Older revision		Revision as of 11:18, 25 September 2018
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	== Ligand specificities ==		== Ligand specificities ==
−	Family 73 CBMs are modules of approximately 60 residues that are appended to bacterial enzymes associated to chitin degradation <cite>Forsberg2016 Wong2012 Tuveng2016</cite>. Binding to amorphous and crystalline α- and β-chitin has been demonstrated <cite>Forsberg2016 Wong2012</cite>. The CBM73 module of the tri-modular LPMO ,''Cj''LPMO10A, binds tightly to α- chitin (Kd = 4.3 µM) and binding equilibrium is established within 15 minutes after mixing the protein and substrate <cite>Forsberg2016</cite>.	+	Family 73 CBMs are modules of approximately 60 residues that are appended to bacterial enzymes associated to chitin degradation <cite>Forsberg2016 Wong2012 Tuveng2016</cite>. Binding to amorphous and crystalline α- and β-chitin has been demonstrated <cite>Forsberg2016 Wong2012</cite>. The CBM73 module of the tri-modular LPMO, ''Cj''LPMO10A, binds tightly to α- chitin (Kd = 4.3 µM) and binding equilibrium is established within 15 minutes after mixing the protein and substrate <cite>Forsberg2016</cite>.

← Older revision		Revision as of 11:16, 25 September 2018
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	== Ligand specificities ==		== Ligand specificities ==
−	Family 73 CBMs are modules of approximately 60 residues that are appended to bacterial enzymes associated to chitin degradation <cite>Forsberg2016 Wong2012 Tuveng2016</cite>. Binding to amorphous and crystalline α- and β-chitin has been demonstrated <cite>Forsberg2016 Wong2012</cite>. The CBM73 module of the tri-modular LPMO ''Cj''LPMO10A binds tightly to α- chitin (Kd = 4.3 µM) and binding equilibrium is established within 15 minutes after mixing the protein and substrate <cite>Forsberg2016</cite>.	+	Family 73 CBMs are modules of approximately 60 residues that are appended to bacterial enzymes associated to chitin degradation <cite>Forsberg2016 Wong2012 Tuveng2016</cite>. Binding to amorphous and crystalline α- and β-chitin has been demonstrated <cite>Forsberg2016 Wong2012</cite>. The CBM73 module of the tri-modular LPMO ,''Cj''LPMO10A, binds tightly to α- chitin (Kd = 4.3 µM) and binding equilibrium is established within 15 minutes after mixing the protein and substrate <cite>Forsberg2016</cite>.

← Older revision		Revision as of 11:10, 25 September 2018
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	== Ligand specificities ==		== Ligand specificities ==
−	Family 73 CBMs are modules of approximately 60 residues that are appended to bacterial enzymes associated to chitin degradation <cite>Forsberg2016 Wong2012 Tuveng2016</cite>. Binding to amorphous and crystalline α- and β-chitin has been demonstrated <cite>Forsberg2016 Wong2012</cite>.~~Using a solid state depletion assay, the~~ CBM73 module of the tri-modular LPMO ''Cj''LPMO10A ~~was shown~~ to ~~have a dissociation constant~~ (Kd~~) of~~ 4.3 µM ~~for~~ binding ~~to α- chitin~~ <cite>Forsberg2016</cite>.	+	Family 73 CBMs are modules of approximately 60 residues that are appended to bacterial enzymes associated to chitin degradation <cite>Forsberg2016 Wong2012 Tuveng2016</cite>. Binding to amorphous and crystalline α- and β-chitin has been demonstrated <cite>Forsberg2016 Wong2012</cite>. The CBM73 module of the tri-modular LPMO ''Cj''LPMO10A binds tightly to α- chitin (Kd = 4.3 µM) and binding equilibrium is established within 15 minutes after mixing the protein and substrate <cite>Forsberg2016</cite>.

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 Currently no NMR or crystal structure is available for CBM73s, but circular dichroism experiments of the CBM from the ''Vibrio cholera'' GlcNAc-binding protein (GbpA, VcLPMO10B) indicated a  β-sheet containing structure <cite>Wong2012</cite>. Sequence alignment shows that the CBM73 are distantly related to chitin-binding modules belonging to the [[CBM5]] family  ([[Carbohydrate-binding_modules#Types|type A]]). Despite low sequence similarity, conserved aromatic amino acids within the [[CBM5]] family, responsible for substrate-binding <cite>Akagi2006</cite>, align well with similar residues in the CBM73 family (Figure 1A)<cite>Forsberg2016 Tuveng2016</cite>. Two additional aromatic residues are found in the CBM73 family compared to the CBM5 family. Compatibly, a somewhat lower ''K''d for α-chitin was observed for the C-terminal CBM73 of the ''Cellvibrio japonicus'' LPMO (''Cj''LPMO10A) relative to its internal CBM5 (Figure 1BC)<cite>Forsberg2016</cite>.
-[[Image:CBM73 fig1.png|thumb|right|600px|'''Figure 1.''' (A) Multiple sequence alignment of CBM5s (grey) and CBM73s (yellow) from ''Cellvibrio japonicus'' (Cj), ''Cellvibrio mixus'' (Cm) and ''Streptomyces griseus'' (Sg). Conserved aromatic residues are labelled white on a blue background and the disulfide in CBM5s are shown above the alignment (S-S). (B) Modular organization of ''C. japonicus'' CBM73 containing enzymes. (C) Comparative binding of the CBMs from the ''C. japonicus'' LPMO (CjLPMO10A). Dissociation constants of 5.3 µM and 4.3 µM was obtained for α-chitin for the CBM5 and the CBM73, respectively <cite>Forsberg2016</cite>. The figure was adapted from Forsberg et al. <cite>Forsberg2016</cite>.          ]]
+[[Image:CBM73 fig1.png|thumb|right|600px|'''Figure 1.''' (A) Multiple sequence alignment of CBM5s (grey) and CBM73s (yellow) from ''Cellvibrio japonicus'' (Cj), ''Cellvibrio mixus'' (Cm) and ''Streptomyces griseus'' (Sg). Conserved aromatic residues are labelled white on a blue background and the disulfide in CBM5s are shown above the alignment (S-S). (B) Modular organization of ''C. japonicus'' CBM73 containing enzymes. (C) Comparative binding of the CBMs from the ''C. japonicus'' LPMO (CjLPMO10A). Dissociation constants of 5.3 µM and 4.3 µM was obtained for α-chitin for the CBM5 and the CBM73, respectively <cite>Forsberg2016</cite> , determined by solid state depletion assays. The figure was adapted from Forsberg et al. <cite>Forsberg2016</cite>.          ]]
 == Functionalities ==

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 == Family Firsts ==
 ;First Identified
-:Family CBM73 was first found as a C-terminal module of the tri-modular ''Cellvibrio japonicus'' chitin-oxidizing LPMO (AA10-CBM5-CBM73) <cite>Forsberg2016</cite>.
+:Family CBM73 was first found as a C-terminal module of the tri-modular ''Cellvibrio japonicus'' chitin-oxidizing LPMO ([[AA10]]-[[CBM5]]-CBM73) <cite>Forsberg2016</cite>.
 ;First Structural Characterization