1oh3
From Proteopedia
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(New page: 200px<br /> <applet load="1oh3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oh3, resolution 1.50Å" /> '''E78R MUTANT OF A CA...)
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Revision as of 19:30, 29 October 2007
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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]. 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
Page seeded by OCA on Mon Oct 29 21:35:24 2007
