2bjf: Difference between revisions
New page: left|200px<br /> <applet load="2bjf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bjf, resolution 1.67Å" /> '''CRYSTAL STRUCTURE O... |
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==About this Structure== | ==About this Structure== | ||
2BJF is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]] with DXC, TAU and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.24 3.5.1.24]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BJF OCA]]. | 2BJF is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]] with DXC, TAU and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Choloylglycine_hydrolase Choloylglycine hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.24 3.5.1.24]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BJF OCA]]. | ||
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15823032 15823032] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15823032 15823032] | ||
[[Category: Choloylglycine hydrolase]] | |||
[[Category: Clostridium perfringens]] | [[Category: Clostridium perfringens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ntn-hydrolase]] | [[Category: ntn-hydrolase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:12:03 2007'' | ||
Revision as of 14:07, 30 October 2007
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CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE
OverviewOverview
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., ... [(full description)]
About this StructureAbout this Structure
2BJF is a [Single protein] structure of sequence from [Clostridium perfringens] with DXC, TAU and GOL as [ligands]. Active as [Choloylglycine hydrolase], with EC number [3.5.1.24]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
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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