Carbohydrate Binding Module Family 5 - Revision history

Elizabeth Ficko-Blean at 13:55, 2 May 2024

2024-05-02T13:55:13Z

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

2021-12-18T21:19:09Z

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

Appa Rao Podile at 11:34, 10 June 2020

2020-06-10T11:34:38Z

Manjeet Kaur at 07:23, 7 June 2020

2020-06-07T07:23:20Z

Manjeet Kaur at 07:17, 7 June 2020

2020-06-07T07:17:58Z

Manjeet Kaur at 07:11, 7 June 2020

2020-06-07T07:11:47Z

Manjeet Kaur at 07:06, 7 June 2020

2020-06-07T07:06:29Z

Manjeet Kaur at 07:05, 7 June 2020

2020-06-07T07:05:49Z

Manjeet Kaur at 06:40, 7 June 2020

2020-06-07T06:40:36Z

Elizabeth Ficko-Blean at 13:44, 3 June 2020

2020-06-03T13:44:21Z

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 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 |-
-| colspan="2" |{{CAZyDBlink}}CBM05.html
+| colspan="2" |{{CAZyDBlink}}CBM5.html
 |}
 </div>

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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]]: ^^^Manjeet Kaur^^^
+* [[Author]]: [[User:Manjeet Kaur|Manjeet Kaur]]
-* [[Responsible Curator]]:  ^^^Appa Rao Podile^^^
+* [[Responsible Curator]]:  [[User:Appa Rao Podile|Appa Rao Podile]]
 ----

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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]]: ^^^Manjeet Kaur^^^
 * [[Responsible Curator]]:  ^^^Appa Rao Podile^^^

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 == Family Firsts ==
-;First indentified: CBM5 modules were first discovered in Endoglucanase, CBDEGZ from ''Erwinia chrysanthemi'' <cite>Brun1997</cite>.
+;First indentified: CBM5 modules were first discovered in Endoglucanase, CBDEGZ from ''Erwinia chrysanthemi'' (''Ec''EGZCBM5) <cite>Brun1997</cite>.
-;First structural characterization: The first NMR derived structure of CBM5 was from CBDEGZ [{{PDBlink}}1AIW PDB ID 1AIW] <cite>Brun1997</cite> and first crystal structure was studied for ChBDChiB from ''Serratia marcescens'' (''Sm''ChiBCBM5) [{{PDBlink}}1E15 PDB ID 1E15] <cite>Van2000</cite>.
+;First structural characterization: The first NMR derived structure of CBM5 was from ''Ec''EGZCBM5 [{{PDBlink}}1AIW PDB ID 1AIW] <cite>Brun1997</cite> and first crystal structure was studied for ChBDChiB from ''Serratia marcescens'' (''Sm''ChiBCBM5) [{{PDBlink}}1E15 PDB ID 1E15] <cite>Van2000</cite>.
 == References ==

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 == Functionalities ==
-Multi-modular enzymes like endo-glucanases, chitinases and LPMOs possess CBM5 modules as accessory domains appended to their catalytic domain, either directly or with the help of linkers like FnIII domains <cite>Kezuka2006 Van2000 Uni2012 Manjeet2013 Brun1997 Forsberg2016 Mutahir2018 Manjeet2019</cite>. The CBM5 domains are responsible for increased affinity of these enzymes towards crystalline cellulose or chitin. Their presence also increases the efficiency of enzymes to bind to substrates in a broader pH range <cite>Uni2012 Manjeet2019</cite>. Deletion of the CBM5 resulted in reduction or complete loss of binding in several instances <cite>Manjeet2013</cite>. Deletion of C-terminal FnIII and CBM5 domains from BliChi resulted in 5-fold reduction of hydrolytic activity on β-chitin and the mutant was unable to degrade α-chitin <cite>Manjeet2013</cite>. Accessory domains have thus been suggested to play an important role in hydrolysis by moving the enzymes in close proximity of substrates <cite>Manjeet2019</cite>. Presence of CBM5 domains in LPMOs have been shown to alter the product profile while acting on crystalline β-chitin substrates <cite>Manjeet2019</cite>. In ''Bc''LPMO10A, CBM5 promoted substrate binding as well as protected the enzyme from inactivation <cite>Mutahir2018</cite>.
+Multi-modular enzymes like endo-glucanases, chitinases and LPMOs possess CBM5 modules as accessory domains appended to their catalytic domain, either directly or with the help of linkers like FnIII domains <cite>Kezuka2006 Van2000 Uni2012 Manjeet2013 Brun1997 Forsberg2016 Mutahir2018 Manjeet2019</cite>. The CBM5 domains are responsible for increased affinity of these enzymes towards crystalline cellulose or chitin. Their presence also increases the efficiency of enzymes to bind to substrates in a broader pH range <cite>Uni2012 Manjeet2019</cite>. Deletion of the CBM5 resulted in reduction or complete loss of binding in several instances <cite>Manjeet2013</cite>. Deletion of C-terminal FnIII and CBM5 domains from ''Bli''Chi resulted in 5-fold reduction of hydrolytic activity on β-chitin and the mutant was unable to degrade α-chitin <cite>Manjeet2013</cite>. Accessory domains have thus been suggested to play an important role in hydrolysis by moving the enzymes in close proximity of substrates <cite>Manjeet2019</cite>. Presence of CBM5 domains in LPMOs have been shown to alter the product profile while acting on crystalline β-chitin substrates <cite>Manjeet2019</cite>. In ''Bc''LPMO10A, CBM5 promoted substrate binding as well as protected the enzyme from inactivation <cite>Mutahir2018</cite>.
 == Family Firsts ==

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 The three structures revealed that CBM5s are composed of five β-strands (β1-5) <cite>Kezuka2006 Van2000 Brun1997</cite>. The β1, β2 and β3 forms the principle structure and the additional short β-strands (β4 and β5) form an antiparallel β-sheet which is independent of the main strand. The ''Ec''EGZCBM5 resembles a ski-boot or L-shaped structure composed of only β-sheets <cite>Brun1997</cite>. Helix structures have not been found in CBM5 modules.
-There are a few differences in CBM5 structures from endo-glucanases (''Ec''EGZCBM5) and chitinases (''Sm''ChiBCBM5 and ''Sg''ChiCCBM5). The ''Ec''EGZCBM5 possesses a conserved disulfide bond between Cys4 and Cys61 <cite>Brun1997</cite>. These disulfide bonds have not been reported in ''Sm''ChiBCBM5 and ''Sg''ChiCCBM5 <cite>Kezuka2006 Van2000</cite>.
+There are a few differences in CBM5 structures from endo-glucanases (''Ec''EGZCBM5) and chitinases (''Sm''ChiBCBM5 and ''Sg''ChiCCBM5). The ''Ec''EGZCBM5 possesses a conserved disulfide bond between Cys4 and Cys61 (Figure 1) <cite>Brun1997</cite>. These disulfide bonds have not been reported in ''Sm''ChiBCBM5 and ''Sg''ChiCCBM5 <cite>Kezuka2006 Van2000</cite>.
 CBM5 modules possess surface exposed aromatic residues which interact with polysaccharides most probably through hydrophobic interactions <cite>Kezuka2006 Simpson1999</cite>. These aromatic residues form a flat platform to bind to the planar surfaces of crystalline cellulose/chitin. CBM5 are thus classified under [[Carbohydrate-binding_modules#Types|type A]] CBMs <cite>Gilbert2013</cite>. The ''Ec''EGZCBM5 [{{PDBlink}}1AIW PDB ID 1AIW]  possesses three exposed aromatic residues: Trp18, Trp43 and Tyr44 (Figure 1). Trp18 is present on an extra loop, is linearly aligned to Trp43 and Tyr44 and extends the substrate binding site <cite>Brun1997</cite>. The three residues are essential for complete binding of ''Ec''EGZCBM5. Polar residues like Asp17 are present on the cellulose binding face and form H-bonds to stabilize the appropriate orientation of cellulose binding residues <cite>Brun1997</cite>. Polar residues also form H-bonds with oxygen atoms and/or OH-groups of glucose subunits of cellulose and thus have been proposed to play a role in cellulose-disruption <cite>Brun1997</cite>. Mutation of Asp17 resulted in decreased binding towards cellulose <cite>Simpson1999</cite>.

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 == Structural Features ==
-[[File:Figure 1 EcEcEGZCBM5.png|thumb|300px|right|'''Figure 1.''' CBM5 of an endoglucanase from ''Erwinia chrysanthemi'' [{{PDBlink}}1AIW PDB ID 1AIW] showing surface exposed aromatic residues (Trp18, Trp43 and Tyr44) and a conserved disulfide bond between Cys4 and Cys61.]]
+[[File:Figure 1 EcEGZCBM5.png|thumb|300px|right|'''Figure 1.''' CBM5 of an endoglucanase from ''Erwinia chrysanthemi'' [{{PDBlink}}1AIW PDB ID 1AIW] showing surface exposed aromatic residues (Trp18, Trp43 and Tyr44) and a conserved disulfide bond between Cys4 and Cys61.]]
 The structures of CBM5 domains have been elucidated for an endoglucanase, CBDEGZ from ''Erwinia chrysanthemi'' (''Ec''EGZCBM5) and two chitinases, ChBDChiB from ''Serratia marcescens'' (''Sm''ChiBCBM5) and ChBDChiC from ''Streptomyces griseus'' HUT6037 (''Sg''ChiCCBM5) <cite>Kezuka2006 Van2000 Brun1997</cite>.

← Older revision		Revision as of 07:05, 7 June 2020
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	== Structural Features ==		== Structural Features ==
		+	[[File:Figure 1 EcEcEGZCBM5.png\|thumb\|300px\|right\|'''Figure 1.''' CBM5 of an endoglucanase from ''Erwinia chrysanthemi'' [{{PDBlink}}1AIW PDB ID 1AIW] showing surface exposed aromatic residues (Trp18, Trp43 and Tyr44) and a conserved disulfide bond between Cys4 and Cys61.]]
	The structures of CBM5 domains have been elucidated for an endoglucanase, CBDEGZ from ''Erwinia chrysanthemi'' (''Ec''EGZCBM5) and two chitinases, ChBDChiB from ''Serratia marcescens'' (''Sm''ChiBCBM5) and ChBDChiC from ''Streptomyces griseus'' HUT6037 (''Sg''ChiCCBM5) <cite>Kezuka2006 Van2000 Brun1997</cite>.		The structures of CBM5 domains have been elucidated for an endoglucanase, CBDEGZ from ''Erwinia chrysanthemi'' (''Ec''EGZCBM5) and two chitinases, ChBDChiB from ''Serratia marcescens'' (''Sm''ChiBCBM5) and ChBDChiC from ''Streptomyces griseus'' HUT6037 (''Sg''ChiCCBM5) <cite>Kezuka2006 Van2000 Brun1997</cite>.

← Older revision		Revision as of 06:40, 7 June 2020
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	== Structural Features ==		== Structural Features ==
−	[[File:EcEGZCBM5.png\|thumb\|300px\|right\|'''Figure 1.''' CBM5 of an endoglucanase from ''Erwinia chrysanthemi'' [{{PDBlink}}1AIW PDB ID 1AIW] showing surface exposed aromatic residues; Trp18, Trp43 and Tyr44.]]
−
	The structures of CBM5 domains have been elucidated for an endoglucanase, CBDEGZ from ''Erwinia chrysanthemi'' (''Ec''EGZCBM5) and two chitinases, ChBDChiB from ''Serratia marcescens'' (''Sm''ChiBCBM5) and ChBDChiC from ''Streptomyces griseus'' HUT6037 (''Sg''ChiCCBM5) <cite>Kezuka2006 Van2000 Brun1997</cite>.		The structures of CBM5 domains have been elucidated for an endoglucanase, CBDEGZ from ''Erwinia chrysanthemi'' (''Ec''EGZCBM5) and two chitinases, ChBDChiB from ''Serratia marcescens'' (''Sm''ChiBCBM5) and ChBDChiC from ''Streptomyces griseus'' HUT6037 (''Sg''ChiCCBM5) <cite>Kezuka2006 Van2000 Brun1997</cite>.