1GWM
Carbohydrate binding module family29 complexed with glucohexaose
1GWM の概要
エントリーDOI | 10.2210/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 | |
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: 12391332DOI: 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) |
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