2BJF
Crystal Structure of Conjugated Bile Acid Hydrolase from Clostridium perfringens in Complex with Reaction Products Taurine and Deoxycholate
Summary for 2BJF
| Entry DOI | 10.2210/pdb2bjf/pdb |
| Related | 2BJG |
| Descriptor | CHOLOYLGLYCINE HYDROLASE, (3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID, 2-AMINOETHANESULFONIC ACID, ... (5 entities in total) |
| Functional Keywords | amidohydrolase, ntn-hydrolase, bile acids, hydrolase, bsh |
| Biological source | CLOSTRIDIUM PERFRINGENS |
| Total number of polymer chains | 1 |
| Total formula weight | 37923.03 |
| Authors | Rossocha, M.,Schultz-Heienbrok, R.,Von Moeller, H.,Coleman, J.P.,Saenger, W. (deposition date: 2005-02-02, release date: 2005-03-03, Last modification date: 2023-12-13) |
| Primary citation | 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 Cited by 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: 15823032DOI: 10.1021/BI0473206 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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