1O8S

Structure of CsCBM6-3 from Clostridium stercorarium in complex with cellobiose

1O8S の概要

• エントリーDOI: 10.2210/pdb1o8s/pdb
• 関連するPDBエントリー: 1O8P 1OD3
• 関連するBIRD辞書のPRD_ID: PRD_900005
• 分子名称: PUTATIVE ENDO-XYLANASE, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, carbohydrate-binding module, xylan, cellulose, beta- sandwich, glycosidase, xylan degradation
• 由来する生物種: CLOSTRIDIUM STERCORARIUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17788.32

構造登録者

Boraston, A.B.,Notenboom, V.,Warren, R.A.J.,Kilbrun, D.G.,Rose, D.R.,Davies, G.J. (登録日: 2002-11-28, 公開日: 2003-03-13, 最終更新日: 2023-12-13)

主引用文献

Boraston, A.B.,Notenboom, V.,Warren, R.A.J.,Kilburn, D.G.,Rose, D.R.,Davies, G.J.
Structure and Ligand Binding of Carbohydrate-Binding Module Cscbm6-3 Reveals Similarities with Fucose-Specific Lectins and Galactose-Binding Domains
J.Mol.Biol., 327:659-, 2003

PubMed Abstract: Carbohydrate-binding polypeptides, including carbohydrate-binding modules (CBMs) from polysaccharidases, and lectins, are widespread in nature. Whilst CBMs are classically considered distinct from lectins, in that they are found appended to polysaccharide-degrading enzymes, this distinction is blurring. The crystal structure of CsCBM6-3, a "sequence-family 6" CBM in a xylanase from Clostridium stercorarium, at 2.3 A reveals a similar, all beta-sheet fold to that from MvX56, a module found in a family 33 glycoside hydrolase sialidase from Micromonospora viridifaciens, and the lectin AAA from Anguilla anguilla. Sequence analysis leads to the classification of MvX56 and AAA into a family distinct from that containing CsCBM6-3. Whilst these polypeptides are similar in structure they have quite different carbohydrate-binding specificities. AAA is known to bind fucose; CsCBM6-3 binds cellulose, xylan and other beta-glucans. Here we demonstrate that MvX56 binds galactose, lactose and sialic acid. Crystal structures of CsCBM6-3 in complex with xylotriose, cellobiose, and laminaribiose, 2.0 A, 1.35 A, and 1.0 A resolution, respectively, reveal that the binding site of CsCBM6-3 resides on the same polypeptide face as for MvX56 and AAA. Subtle differences in the ligand-binding surface give rise to the different specificities and biological activities, further blurring the distinction between classical lectins and CBMs.

PubMed: 12634060
DOI: 10.1016/S0022-2836(03)00152-9

実験手法

X-RAY DIFFRACTION (1.15 Å)