Loading
PDBj
メニューPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1GWM

Carbohydrate binding module family29 complexed with glucohexaose

1GWM の概要
エントリーDOI10.2210/pdb1gwm/pdb
関連するPDBエントリー1GWK 1GWL
分子名称NON-CATALYTIC PROTEIN 1, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-alpha-D-glucopyranose, COBALT (II) ION, ... (5 entities in total)
機能のキーワードcarbohydrate binding domain, glucomannan, cellohexaose, mannohexaose, cellulosome
由来する生物種PIROMYCES EQUI
タンパク質・核酸の鎖数1
化学式量合計18809.39
構造登録者
Charnock, S.J.,Nurizzo, D.,Davies, G.J. (登録日: 2002-03-19, 公開日: 2003-03-20, 最終更新日: 2024-05-01)
主引用文献Charnock, S.J.,Bolam, D.,Nurizzo, D.,Szabo, L.,Mckie, V.,Gilbert, H.,Davies, G.J.
Promiscuity in Ligand-Binding: The Three-Dimensional Structure of a Piromyces Carbohydrate-Binding Module,Cbm29-2,in Complex with Cello- and Mannohexaose
Proc.Natl.Acad.Sci.USA, 99:14077-, 2002
Cited by
PubMed Abstract: Carbohydrate-protein recognition is central to many biological processes. Enzymes that act on polysaccharide substrates frequently contain noncatalytic domains, "carbohydrate-binding modules" (CBMs), that target the enzyme to the appropriate substrate. CBMs that recognize specific plant structural polysaccharides are often able to accommodate both the variable backbone and the side-chain decorations of heterogeneous ligands. "CBM29" modules, derived from a noncatalytic component of the Piromyces equi cellulase/hemicellulase complex, provide an example of this selective yet flexible recognition. They discriminate strongly against some polysaccharides while remaining relatively promiscuous toward both beta-1,4-linked manno- and cello-oligosaccharides. This feature may reflect preferential, but flexible, targeting toward glucomannans in the plant cell wall. The three-dimensional structure of CBM29-2 and its complexes with cello- and mannohexaose reveal a beta-jelly-roll topology, with an extended binding groove on the concave surface. The orientation of the aromatic residues complements the conformation of the target sugar polymer while accommodation of both manno- and gluco-configured oligo- and polysaccharides is conferred by virtue of the plasticity of the direct interactions from their axial and equatorial 2-hydroxyls, respectively. Such flexible ligand recognition targets the anaerobic fungal complex to a range of different components in the plant cell wall and thus plays a pivotal role in the highly efficient degradation of this composite structure by the microbial eukaryote.
PubMed: 12391332
DOI: 10.1073/PNAS.212516199
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.15 Å)
構造検証レポート
Validation report summary of 1gwm
検証レポート(詳細版)ダウンロードをダウンロード

226707

件を2024-10-30に公開中

PDB statisticsPDBj update infoContact PDBjnumon