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1od3

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(New page: 200px<br /> <applet load="1od3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1od3, resolution 1.00&Aring;" /> '''STRUCTURE OF CSCBM6...)
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Revision as of 18:44, 29 October 2007


1od3, resolution 1.00Å

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

Overview

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 ... [(full description)]

About this Structure

1OD3 is a [Single protein] structure of sequence from [Clostridium stercorarium] with CA and ACY as [ligands]. Full crystallographic information is available from [OCA].

Reference

Structure and ligand binding of carbohydrate-binding module CsCBM6-3 reveals similarities with fucose-specific lectins and "galactose-binding" domains., Boraston AB, Notenboom V, Warren RA, Kilburn DG, Rose DR, Davies G, J Mol Biol. 2003 Mar 28;327(3):659-69. PMID:12634060

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