2bjg
From Proteopedia
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| - | [[Image:2bjg.gif|left|200px]]<br /><applet load="2bjg" size=" | + | [[Image:2bjg.gif|left|200px]]<br /><applet load="2bjg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bjg, resolution 2.10Å" /> | caption="2bjg, resolution 2.10Å" /> | ||
'''CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE'''<br /> | '''CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BJG 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 EDO as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=AC1:Edo Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2BJG 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 <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ntn-hydrolase]] | [[Category: ntn-hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:24:53 2008'' |
Revision as of 08:24, 3 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
2BJG is a Single protein structure of sequence from Clostridium perfringens with as ligand. 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
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