2BJF

Crystal Structure of Conjugated Bile Acid Hydrolase from Clostridium perfringens in Complex with Reaction Products Taurine and Deoxycholate

2BJF の概要

• エントリーDOI: 10.2210/pdb2bjf/pdb
• 関連するPDBエントリー: 2BJG
• 分子名称: CHOLOYLGLYCINE HYDROLASE, (3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID, 2-AMINOETHANESULFONIC ACID, ... (5 entities in total)
• 機能のキーワード: amidohydrolase, ntn-hydrolase, bile acids, hydrolase, bsh
• 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: 37923.03

構造登録者

Rossocha, M.,Schultz-Heienbrok, R.,Von Moeller, H.,Coleman, J.P.,Saenger, W. (登録日: 2005-02-02, 公開日: 2005-03-03, 最終更新日: 2023-12-13)

主引用文献

Rossocha, M.,Schultz-Heienbrok, R.,Von Moeller, H.,Coleman, J.P.,Saenger, W.
Conjugated Bile Acid Hydrolase is a Tetrameric N-Terminal Thiol Hydrolase with Specific Recognition of its Cholyl But not of its Tauryl Product
Biochemistry, 44:5739-, 2005

PubMed Abstract: Bacterial bile salt hydrolases catalyze the degradation of conjugated bile acids in the mammalian gut. The crystal structures of conjugated bile acid hydrolase (CBAH) from Clostridium perfringens as apoenzyme and in complex with taurodeoxycholate that was hydrolyzed to the reaction products taurine and deoxycholate are described here at 2.1 and 1.7 A resolution, respectively. The crystal structures reveal close relationship between CBAH and penicillin V acylase from Bacillus sphaericus. This similarity together with the N-terminal cysteine classifies CBAH as a member of the N-terminal nucleophile (Ntn) hydrolase superfamily. Both crystal structures show an identical homotetrameric organization with dihedral (D(2) or 222) point group symmetry. The structure analysis of C. perfringens CBAH identifies critical residues in catalysis, substrate recognition, and tetramer formation which may serve in further biochemical characterization of bile acid hydrolases.

PubMed: 15823032
DOI: 10.1021/BI0473206

実験手法

X-RAY DIFFRACTION (1.67 Å)