1od3: Difference between revisions

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{{STRUCTURE_1od3|  PDB=1od3  |  SCENE=  }}  
{{STRUCTURE_1od3|  PDB=1od3  |  SCENE=  }}  


'''STRUCTURE OF CSCBM6-3 FROM CLOSTRIDIUM STERCORARIUM IN COMPLEX WITH LAMINARIBIOSE'''
===STRUCTURE OF CSCBM6-3 FROM CLOSTRIDIUM STERCORARIUM IN COMPLEX WITH LAMINARIBIOSE===




==Overview==
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Carbohydrate-binding polypeptides, including carbohydrate-binding modules (CBMs) from polysaccharidases, and lectins, are widespread in nature. Whilst CBMs are classically considered distinct from lectins, in that they are found appended to polysaccharide-degrading enzymes, this distinction is blurring. The crystal structure of CsCBM6-3, a "sequence-family 6" CBM in a xylanase from Clostridium stercorarium, at 2.3 A reveals a similar, all beta-sheet fold to that from MvX56, a module found in a family 33 glycoside hydrolase sialidase from Micromonospora viridifaciens, and the lectin AAA from Anguilla anguilla. Sequence analysis leads to the classification of MvX56 and AAA into a family distinct from that containing CsCBM6-3. Whilst these polypeptides are similar in structure they have quite different carbohydrate-binding specificities. AAA is known to bind fucose; CsCBM6-3 binds cellulose, xylan and other beta-glucans. Here we demonstrate that MvX56 binds galactose, lactose and sialic acid. Crystal structures of CsCBM6-3 in complex with xylotriose, cellobiose, and laminaribiose, 2.0 A, 1.35 A, and 1.0 A resolution, respectively, reveal that the binding site of CsCBM6-3 resides on the same polypeptide face as for MvX56 and AAA. Subtle differences in the ligand-binding surface give rise to the different specificities and biological activities, further blurring the distinction between classical lectins and CBMs.
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{{ABSTRACT_PUBMED_12634060}}


==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Laminaribiose]]
[[Category: Laminaribiose]]
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