1GUI

CBM4 structure and function

1GUI の概要

• エントリーDOI: 10.2210/pdb1gui/pdb
• 分子名称: LAMINARINASE 16A, beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: carbohydrate binding module, cbm, glucan, cellulose
• 由来する生物種: THERMOTOGA MARITIMA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19105.46

構造登録者

Nurizzo, D.,Notenboom, V.,Davies, G.J. (登録日: 2002-01-27, 公開日: 2002-09-26, 最終更新日: 2023-12-13)

主引用文献

Boraston, A.B.,Nurizzo, D.,Notenboom, V.,Ducros, V.,Rose, D.R.,Kilburn, D.G.,Davies, G.J.
Differential Oligosaccharide Recognition by Evolutionarily-Related Beta-1,4 and Beta-1,3 Glucan-Binding Modules
J.Mol.Biol., 319:1143-, 2002

PubMed Abstract: Enzymes active on complex carbohydrate polymers frequently have modular structures in which a catalytic domain is appended to one or more carbohydrate-binding modules (CBMs). Although CBMs have been classified into a number of families based upon sequence, many closely related CBMs are specific for different polysaccharides. In order to provide a structural rationale for the recognition of different polysaccharides by CBMs displaying a conserved fold, we have studied the thermodynamics of binding and three-dimensional structures of the related family 4 CBMs from Cellulomonas fimi Cel9B and Thermotoga maritima Lam16A in complex with their ligands, beta-1,4 and beta-1,3 linked gluco-oligosaccharides, respectively. These two CBMs use a structurally conserved constellation of aromatic and polar amino acid side-chains that interact with sugars in two of the five binding subsites. Differences in the length and conformation of loops in non-conserved regions create binding-site topographies that complement the known solution conformations of their respective ligands. Thermodynamics interpreted in the light of structural information highlights the differential role of water in the interaction of these CBMs with their respective oligosaccharide ligands.

PubMed: 12079353
DOI: 10.1016/S0022-2836(02)00374-1

実験手法

X-RAY DIFFRACTION (1.9 Å)