2W1Q

Unique ligand binding specificity for a family 32 Carbohydrate- Binding Module from the Mu toxin produced by Clostridium perfringens

2W1Q の概要

• エントリーDOI: 10.2210/pdb2w1q/pdb
• 関連するPDBエントリー: 2W1S 2W1U 2WDB
• 分子名称: HYALURONOGLUCOSAMINIDASE, CALCIUM ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: family 32 carbohydrate binding module, glycosidase, glycoside hydrolase, clostridium perfringens, cbm, toxin, secreted, virulence, hydrolase
• 由来する生物種: CLOSTRIDIUM PERFRINGENS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43126.49

構造登録者

Ficko-Blean, E.,Boraston, A.B. (登録日: 2008-10-20, 公開日: 2009-05-05, 最終更新日: 2024-05-08)

主引用文献

Ficko-Blean, E.,Boraston, A.B.
N-Acetylglucosamine Recognition by a Family 32 Carbohydrate-Binding Module from Clostridium Perfringens Nagh.
J.Mol.Biol., 390:208-, 2009

PubMed Abstract: Many carbohydrate-active enzymes have complex architectures comprising multiple modules that may be involved in catalysis, carbohydrate binding, or protein-protein interactions. Carbohydrate-binding modules (CBMs) are a common ancillary module whose function is to promote the adherence of the complete enzyme to carbohydrate substrates. CBM family 32 has been proposed to be one of the most diverse CBM families classified to date, yet all of the structurally characterized CBM32s thus far recognize galactose-based ligands. Here, we report a unique binding specificity and mode of ligand binding for a family 32 CBM. NagHCBM32-2 is one of four CBM32 modules in NagH, a family 84 glycoside hydrolase secreted by Clostridium perfringens. NagHCBM32-2 has the beta-sandwich scaffold common to members of the family; however, its specificity for N-acetylglucosamine is unusual among CBMs. X-ray crystallographic analysis of the module at resolutions from 1.45 to 2.0 A and in complex with disaccharides reveals that its mode of sugar recognition is quite different from that observed for galactose-specific CBM32s. This study continues to unravel the diversity of CBMs found in family 32 and how these CBMs might impart the carbohydrate-binding specificity to the extracellular glycoside hydrolases in C. perfringens.

PubMed: 19422833
DOI: 10.1016/J.JMB.2009.04.066

実験手法

X-RAY DIFFRACTION (1.6 Å)