2J1A

Structure of CBM32 from Clostridium perfringens beta-N- acetylhexosaminidase GH84C in complex with galactose

2J1A の概要

• エントリーDOI: 10.2210/pdb2j1a/pdb
• 関連するPDBエントリー: 2CBI 2CBJ 2J1E 2J1F
• 分子名称: HYALURONIDASE, beta-D-galactopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: protein-carbohydrate interaction, glycoside hydrolase, cbm32, gh84c, hydrolase
• 由来する生物種: CLOSTRIDIUM PERFRINGENS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16635.12

構造登録者

Ficko-Blean, E.,Boraston, A.B. (登録日: 2006-08-09, 公開日: 2006-08-22, 最終更新日: 2024-05-08)

主引用文献

Ficko-Blean, E.,Boraston, A.B.
The Interaction of a Carbohydrate-Binding Module from a Clostridium Perfringens N-Acetyl-Beta-Hexosaminidase with its Carbohydrate Receptor
J.Biol.Chem., 281:37748-, 2006

PubMed Abstract: Clostridium perfringens is a notable colonizer of the human gastrointestinal tract. This bacterium is quite remarkable for a human pathogen by the number of glycoside hydrolases found in its genome. The modularity of these enzymes is striking as is the frequent occurrence of modules having amino acid sequence identity with family 32 carbohydrate-binding modules (CBMs), often referred to as F5/8 domains. Here we report the properties of family 32 CBMs from a C. perfringens N-acetyl-beta-hexosaminidase. Macroarray, UV difference, and isothermal titration calorimetry binding studies indicate a preference for the disaccharide LacNAc (beta-d-galactosyl-1,4-beta-d-N-acetylglucosamine). The molecular details of the interaction of this CBM with galactose, LacNAc, and the type II blood group H-trisaccharide are revealed by x-ray crystallographic studies at resolutions of 1.49, 2.4, and 2.3 A, respectively.

PubMed: 16990278
DOI: 10.1074/JBC.M606126200

実験手法

X-RAY DIFFRACTION (1.49 Å)