2bjf

From Proteopedia

(Difference between revisions)

Revision as of 06:35, 16 May 2018

Crystal Structure of Conjugated Bile Acid Hydrolase from Clostridium perfringens in Complex with Reaction Products Taurine and Deoxycholate

Structural highlights

2bjf is a 1 chain structure with sequence from "bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	2bjg
Activity:	Choloylglycine hydrolase, with EC number 3.5.1.24
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CBH_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 PubMed

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.

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

↑ Rossocha M, Schultz-Heienbrok R, von Moeller H, Coleman JP, Saenger W. Conjugated bile acid hydrolase is a tetrameric N-terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product. Biochemistry. 2005 Apr 19;44(15):5739-48. PMID:15823032 doi:http://dx.doi.org/10.1021/bi0473206

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bjf"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF CONJUGATED BILE ACID HYDROLASE FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH REACTION PRODUCTS TAURINE AND DEOXYCHOLATE==
+==Crystal Structure of Conjugated Bile Acid Hydrolase from Clostridium perfringens in Complex with Reaction Products Taurine and Deoxycholate==
 <StructureSection load='2bjf' size='340' side='right' caption='[[2bjf]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bjg|2bjg]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjf OCA], [http://pdbe.org/2bjf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bjf RCSB], [http://www.ebi.ac.uk/pdbsum/2bjf PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjf OCA], [http://pdbe.org/2bjf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bjf RCSB], [http://www.ebi.ac.uk/pdbsum/2bjf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bjf ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bj/2bjf_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bj/2bjf_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2bjf

From Proteopedia

Revision as of 06:35, 16 May 2018

Crystal Structure of Conjugated Bile Acid Hydrolase from Clostridium perfringens in Complex with Reaction Products Taurine and Deoxycholate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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