2bjg

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{{STRUCTURE_2bjg| PDB=2bjg | SCENE= }}
{{STRUCTURE_2bjg| PDB=2bjg | SCENE= }}
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'''CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE'''
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===CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15823032}}
==About this Structure==
==About this Structure==
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[[Category: Cbah]]
[[Category: Cbah]]
[[Category: Ntn-hydrolase]]
[[Category: Ntn-hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:47:55 2008''

Revision as of 05:47, 29 July 2008

Image:2bjg.png

Template:STRUCTURE 2bjg

CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE

Template:ABSTRACT PUBMED 15823032

About this Structure

2BJG is a Single protein structure of sequence from Clostridium perfringens. 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

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