X-ray crystal structure of a non-crystalline cellulose-specific carbohydrate-binding module: CBM28

S Jamal, D Nurizzo, A B Boraston, G J Davies

Research output: Contribution to journalArticlepeer-review

Abstract

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 1.4 Angstrom 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. (C) 2004 Elsevier Ltd. All rights reserved.

Original languageEnglish
Pages (from-to)253-258
Number of pages6
JournalJournal of Molecular Biology
Volume339
Issue number2
DOIs
Publication statusPublished - 28 May 2004

Keywords

  • glycosidase
  • lectin
  • carbohydrate-binding module
  • cellulose
  • glucan
  • ACTIVE ENZYMES
  • RECOGNITION
  • HYDROLYSIS
  • REFINEMENT
  • SUBSTRATE
  • FAMILY
  • MODEL

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