1uww

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spinqualitylabelsall models 1uww, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-RAY CRYSTAL STRUCTURE OF A NON-CRYSTALLINE CELLULOSE SPECIFIC CARBOHYDRATE-BINDING MODULE: CBM28.

Overview

Natural cellulose exists as a composite of different forms, which have, historically been broadly characterized as "crystalline" or "amorphous"., The recognition of both of these forms of cellulose by the, carbohydrate-binding modules (CBM) of microbial glycoside hydrolases is, central to natural and efficient biotechnological conversion of plant cell, wall biomass. There is increasing evidence that, at least some, individual, binding modules target distinct and different regions of non-crystalline, "amorphous" cellulose. Competition experiments show that CBM28 modules do, not compete with CBM17 modules when binding to non-crystalline cellulose., The structure of the BspCBM28 (http://afmb.cnrs-mrs.fr/CAZY/) module from, the Bacillus sp. 1139 family GH5 endoglucanase, comprising a 191 amino, acid protein, has therefore been determined at 1.4A resolution using, single isomorphous replacement with anomalous scattering methods. The, structure reveals a "beta-jelly roll" topology, with high degree of, similarity to the structure of CBM17 domains. Sequence and structural, conservation strongly suggests that these two families of domains have, evolved through gene duplication and subsequent divergence. The, ligand-binding site "topographies" of CBMs from families 28, 17 and 4, begins to shed light on the differential recognition of non-crystalline, cellulose by multi-modular plant cell wall-degrading enzymes.

About this Structure

1UWW is a Single protein structure of sequence from Bacillus sp 1139 with as ligand. Active as Cellulase, with EC number 3.2.1.4 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

X-ray crystal structure of a non-crystalline cellulose-specific carbohydrate-binding module: CBM28., Jamal S, Nurizzo D, Boraston AB, Davies GJ, J Mol Biol. 2004 May 28;339(2):253-8. PMID:15136030

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