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Crystal Structure of Conjugated Bile Acid Hydrolase from Clostridium perfringens in Complex with Reaction Products Taurine and DeoxycholateCrystal Structure of Conjugated Bile Acid Hydrolase from Clostridium perfringens in Complex with Reaction Products Taurine and Deoxycholate
Structural highlights
FunctionCBH_CLOPE The enzyme catalyzes the degradation of conjugated bile acids in the mammalian gut. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBacterial 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. Conjugated bile acid hydrolase is a tetrameric N-terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product.,Rossocha M, Schultz-Heienbrok R, von Moeller H, Coleman JP, Saenger W Biochemistry. 2005 Apr 19;44(15):5739-48. PMID:15823032[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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