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1oh3

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[[Category: ncp1]]
[[Category: ncp1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:08:08 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:54:08 2007''

Revision as of 13:49, 30 October 2007

Image:1oh3.gif

1oh3, resolution 1.50Å

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E78R MUTANT OF A CARBOHYDRATE BINDING MODULE FAMILY 29

Overview

The structural and thermodynamic basis for carbohydrate-protein, recognition is of considerable importance. NCP-1, which is a component of, the Piromyces equi cellulase/hemicellulase complex, presents a provocative, model for analyzing how structural and mutational changes can influence, the ligand specificity of carbohydrate-binding proteins. NCP-1 contains, two "family 29" carbohydrate-binding modules designated CBM29-1 and, CBM29-2, respectively, that display unusually broad specificity; the, proteins interact weakly with xylan, exhibit moderate affinity for, cellulose and mannan, and bind tightly to the beta-1,4-linked, glucose-mannose heteropolymer glucomannan. The crystal structure of, CBM29-2 in complex with cellohexaose and mannohexaose identified key, residues involved in ligand ... [(full description)]

About this Structure

1OH3 is a [Single protein] structure of sequence from [Piromyces equi] with GLC as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Ligand-mediated dimerization of a carbohydrate-binding molecule reveals a novel mechanism for protein-carbohydrate recognition., Flint J, Nurizzo D, Harding SE, Longman E, Davies GJ, Gilbert HJ, Bolam DN, J Mol Biol. 2004 Mar 19;337(2):417-26. PMID:15003456

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