2bjg

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

2bjg is a 2 chain structure with sequence from Clostridium perfringens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:
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/2bjg"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Conjugated Bile Acid Hydrolase from Clostridium perfringens in Complex with Reaction Products Taurine and Deoxycholate==
-<StructureSection load='2bjg' size='340' side='right' caption='[[2bjg]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='2bjg' size='340' side='right'caption='[[2bjg]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bjg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BJG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bjg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BJG FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bjf|2bjf]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2bjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjg OCA], [https://pdbe.org/2bjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bjg RCSB], [https://www.ebi.ac.uk/pdbsum/2bjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bjg ProSAT]</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=2bjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjg OCA], [http://pdbe.org/2bjg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bjg RCSB], [http://www.ebi.ac.uk/pdbsum/2bjg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bjg ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CBH_CLOPE CBH_CLOPE]] The enzyme catalyzes the degradation of conjugated bile acids in the mammalian gut.
+[https://www.uniprot.org/uniprot/CBH_CLOPE CBH_CLOPE] The enzyme catalyzes the degradation of conjugated bile acids in the mammalian gut.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus perfringens veillon and zuber 1898]]
+[[Category: Clostridium perfringens]]
-[[Category: Choloylglycine hydrolase]]
+[[Category: Large Structures]]
-[[Category: Coleman, J P]]
+[[Category: Coleman JP]]
-[[Category: Moeller, H Von]]
+[[Category: Rossocha M]]
-[[Category: Rossocha, M]]
+[[Category: Saenger W]]
-[[Category: Saenger, W]]
+[[Category: Schultz-Heienbrok R]]
-[[Category: Schultz-Heienbrok, R]]
+[[Category: Von Moeller H]]
-[[Category: Amidohydrolase]]
-[[Category: Bile acid]]
-[[Category: Bsh]]
-[[Category: Cbah]]
-[[Category: Hydrolase]]
-[[Category: Ntn-hydrolase]]

2bjg

From Proteopedia

Current revision

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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