2bvd

From Proteopedia

Revision as of 14:44, 30 October 2007

HOW FAMILY 26 GLYCOSIDE HYDROLASES ORCHESTRATE CATALYSIS ON DIFFERENT POLYSACCHARIDES. STRUCTURE AND ACTIVITY OF A CLOSTRIDIUM THERMOCELLUM LICHENASE, CTLIC26A

Overview

One of the most intriguing features of the 90 glycoside hydrolase families, (GHs) is the range of specificities displayed by different members of the, same family, whereas the catalytic apparatus and mechanism are often, invariant. Family GH26 predominantly comprises beta-1,4 mannanases;, however, a bifunctional Clostridium thermocellum GH26 member (hereafter, CtLic26A) displays a markedly different specificity. We show that CtLic26A, is a lichenase, specific for mixed (Glcbeta1,4Glcbeta1,4Glcbeta1,3)n, oligo- and polysaccharides, and displays no activity on manno-configured, substrates or beta-1,4-linked homopolymers of glucose or xylose. The, three-dimensional structure of the native form of CtLic26A has been solved, at 1.50-A resolution, revealing a characteristic (beta/alpha)8 barrel ... [(full description)]

About this Structure

2BVD is a [Single protein] structure of sequence from [Clostridium thermocellum] with ISX as [ligand]. Active as [Cellulase], with EC number [3.2.1.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides: structure and activity of a Clostridium thermocellum lichenase, CtLic26A., Taylor EJ, Goyal A, Guerreiro CI, Prates JA, Money VA, Ferry N, Morland C, Planas A, Macdonald JA, Stick RV, Gilbert HJ, Fontes CM, Davies GJ, J Biol Chem. 2005 Sep 23;280(38):32761-7. Epub 2005 Jun 28. PMID:15987675

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