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1UWW

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

1UWW の概要
エントリーDOI10.2210/pdb1uww/pdb
分子名称ENDOGLUCANASE, CALCIUM ION (3 entities in total)
機能のキーワードcarbohydrate binding module, glycosidase, lectin, cellulose, glucan, cbm, hydrolase
由来する生物種BACILLUS AKIBAI
タンパク質・核酸の鎖数2
化学式量合計43737.32
構造登録者
Jamal, S.,Nurizzo, D.,Boraston, A.,Davies, G.J. (登録日: 2004-02-12, 公開日: 2004-05-13, 最終更新日: 2024-11-06)
主引用文献Jamal, S.,Nurizzo, D.,Boraston, A.,Davies, G.J.
X-Ray Crystal Structure of a Non-Crystalline Cellulose-Specific Carbohydrate-Binding Module: Cbm28
J.Mol.Biol., 339:253-, 2004
Cited by
PubMed 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 1.4A 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.
PubMed: 15136030
DOI: 10.1016/J.JMB.2004.03.069
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.4 Å)
構造検証レポート
Validation report summary of 1uww
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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