2c24: Difference between revisions
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New page: left|200px<br /><applet load="2c24" size="350" color="white" frame="true" align="right" spinBox="true" caption="2c24, resolution 2.27Å" /> '''FAMILY 30 CARBOHYDRA... |
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== | ==FAMILY 30 CARBOHYDRATE-BINDING MODULE OF CELLULOSOMAL CELLULASE CEL9D- CEL44B OF CLOSTRIDIUM THERMOCELLUM== | ||
Enzyme systems that attack the plant cell wall contain noncatalytic | <StructureSection load='2c24' size='340' side='right'caption='[[2c24]], [[Resolution|resolution]] 2.27Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2c24]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C24 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c24 OCA], [https://pdbe.org/2c24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c24 RCSB], [https://www.ebi.ac.uk/pdbsum/2c24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c24 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/P71140_ACETH P71140_ACETH] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enzyme systems that attack the plant cell wall contain noncatalytic carbohydrate-binding modules (CBMs) that mediate attachment to this composite structure and play a pivotal role in maximizing the hydrolytic process. Although xyloglucan, which includes a backbone of beta-1,4-glucan decorated primarily with xylose residues, is a key component of the plant cell wall, CBMs that bind to this polymer have not been identified. Here we showed that the C-terminal domain of the modular Clostridium thermocellum enzyme CtCel9D-Cel44A (formerly known as CelJ) comprises a novel CBM (designated CBM44) that binds with equal affinity to cellulose and xyloglucan. We also showed that accommodation of xyloglucan side chains is a general feature of CBMs that bind to single cellulose chains. The crystal structures of CBM44 and the other CBM (CBM30) in CtCel9D-Cel44A display a beta-sandwich fold. The concave face of both CBMs contains a hydrophobic platform comprising three tryptophan residues that can accommodate up to five glucose residues. The orientation of these aromatic residues is such that the bound ligand would adopt the twisted conformation displayed by cello-oligosaccharides in solution. Mutagenesis studies confirmed that the hydrophobic platform located on the concave face of both CBMs mediates ligand recognition. In contrast to other CBMs that bind to single polysaccharide chains, the polar residues in the binding cleft of CBM44 play only a minor role in ligand recognition. The mechanism by which these proteins are able to recognize linear and decorated beta-1,4-glucans is discussed based on the structures of CBM44 and the other CBMs that bind single cellulose chains. | |||
Xyloglucan is recognized by carbohydrate-binding modules that interact with beta-glucan chains.,Najmudin S, Guerreiro CI, Carvalho AL, Prates JA, Correia MA, Alves VD, Ferreira LM, Romao MJ, Gilbert HJ, Bolam DN, Fontes CM J Biol Chem. 2006 Mar 31;281(13):8815-28. Epub 2005 Nov 28. PMID:16314409<ref>PMID:16314409</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2c24" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glucanase 3D structures|Glucanase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acetivibrio thermocellus]] | |||
[[Category: Large Structures]] | |||
[[Category: Alves VD]] | |||
[[Category: Bolam DN]] | |||
[[Category: Carvalho AL]] | |||
[[Category: Ferreira LMA]] | |||
[[Category: Fontes CMGA]] | |||
[[Category: Gilbert HJ]] | |||
[[Category: Najmudin S]] | |||
[[Category: Prates JAM]] | |||
[[Category: Romao MJ]] | |||
Latest revision as of 13:24, 6 September 2023
FAMILY 30 CARBOHYDRATE-BINDING MODULE OF CELLULOSOMAL CELLULASE CEL9D- CEL44B OF CLOSTRIDIUM THERMOCELLUMFAMILY 30 CARBOHYDRATE-BINDING MODULE OF CELLULOSOMAL CELLULASE CEL9D- CEL44B OF CLOSTRIDIUM THERMOCELLUM
Structural highlights
FunctionPublication Abstract from PubMedEnzyme systems that attack the plant cell wall contain noncatalytic carbohydrate-binding modules (CBMs) that mediate attachment to this composite structure and play a pivotal role in maximizing the hydrolytic process. Although xyloglucan, which includes a backbone of beta-1,4-glucan decorated primarily with xylose residues, is a key component of the plant cell wall, CBMs that bind to this polymer have not been identified. Here we showed that the C-terminal domain of the modular Clostridium thermocellum enzyme CtCel9D-Cel44A (formerly known as CelJ) comprises a novel CBM (designated CBM44) that binds with equal affinity to cellulose and xyloglucan. We also showed that accommodation of xyloglucan side chains is a general feature of CBMs that bind to single cellulose chains. The crystal structures of CBM44 and the other CBM (CBM30) in CtCel9D-Cel44A display a beta-sandwich fold. The concave face of both CBMs contains a hydrophobic platform comprising three tryptophan residues that can accommodate up to five glucose residues. The orientation of these aromatic residues is such that the bound ligand would adopt the twisted conformation displayed by cello-oligosaccharides in solution. Mutagenesis studies confirmed that the hydrophobic platform located on the concave face of both CBMs mediates ligand recognition. In contrast to other CBMs that bind to single polysaccharide chains, the polar residues in the binding cleft of CBM44 play only a minor role in ligand recognition. The mechanism by which these proteins are able to recognize linear and decorated beta-1,4-glucans is discussed based on the structures of CBM44 and the other CBMs that bind single cellulose chains. Xyloglucan is recognized by carbohydrate-binding modules that interact with beta-glucan chains.,Najmudin S, Guerreiro CI, Carvalho AL, Prates JA, Correia MA, Alves VD, Ferreira LM, Romao MJ, Gilbert HJ, Bolam DN, Fontes CM J Biol Chem. 2006 Mar 31;281(13):8815-28. Epub 2005 Nov 28. PMID:16314409[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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