2bjf
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Bacterial bile salt hydrolases catalyze the degradation of conjugated bile | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Clostridium perfringens]] | [[Category: Clostridium perfringens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Coleman, J | + | [[Category: Coleman, J P.]] |
| - | [[Category: Moeller, H | + | [[Category: Moeller, H Von.]] |
[[Category: Rossocha, M.]] | [[Category: Rossocha, M.]] | ||
[[Category: Saenger, W.]] | [[Category: Saenger, W.]] | ||
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[[Category: ntn-hydrolase]] | [[Category: ntn-hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:29 2008'' |
Revision as of 14:38, 21 February 2008
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CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE
Overview
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.
About this Structure
2BJF is a Single protein structure of sequence from Clostridium perfringens with , and as ligands. Active as Choloylglycine hydrolase, with EC number 3.5.1.24 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 16:38:29 2008
