1up2

From Proteopedia

Revision as of 14:02, 30 October 2007

STRUCTURE OF THE ENDOGLUCANASE CEL6 FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH GLUCOSE-ISOFAGOMINE AT 1.9 ANGSTROM

Overview

The genomes of various Mycobacterium tuberculosis strains encode proteins, that do not appear to play a role in the growth or survival of the, bacterium in its mammalian host, including some implicated in plant cell, wall breakdown. Here we show that M. tuberculosis H37Rv does indeed, possess a functional cellulase. The x-ray crystal structure of this, enzyme, in ligand complex forms, from 1.9 to 1.1A resolution, reveals a, highly conserved substrate-binding cleft, which affords similar, and, unusual, distortion of the substrate at the catalytic center. The, endoglucanase activity, together with the existence of a putative, membrane-associated crystalline polysaccharide-binding protein, may, reflect the ancestral soil origin of the Mycobacterium or hint at a, previously unconsidered ... [(full description)]

About this Structure

1UP2 is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with BGC, SO4, ACT, IFM and 1PG as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Mycobacterium tuberculosis strains possess functional cellulases., Varrot A, Leydier S, Pell G, Macdonald JM, Stick RV, Henrissat B, Gilbert HJ, Davies GJ, J Biol Chem. 2005 May 27;280(21):20181-4. Epub 2005 Apr 11. PMID:15824123

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