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==Crystal structure of a 3alpha-hydroxysteroid dehydrogenase (BaiA2) associated with secondary bile acid synthesis from Clostridium scindens VPI12708 in complex with a putative NAD(+)-OH- adduct at 2.0 A resolution==
==Crystal structure of a 3alpha-hydroxysteroid dehydrogenase (BaiA2) associated with secondary bile acid synthesis from Clostridium scindens VPI12708 in complex with a putative NAD(+)-OH- adduct at 2.0 A resolution==
<StructureSection load='4is3' size='340' side='right' caption='[[4is3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4is3' size='340' side='right'caption='[[4is3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4is3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35704 Atcc 35704]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IS3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IS3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4is3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_scindens Clostridium scindens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IS3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4is2|4is2]]</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=4is3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4is3 OCA], [https://pdbe.org/4is3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4is3 RCSB], [https://www.ebi.ac.uk/pdbsum/4is3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4is3 ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">baiA, BAIA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29347 ATCC 35704])</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=4is3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4is3 OCA], [http://pdbe.org/4is3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4is3 RCSB], [http://www.ebi.ac.uk/pdbsum/4is3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4is3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BAIA2_EUBSP BAIA2_EUBSP]] 7-alpha-dehydroxylation of cholic acid and chenodeoxycholate, yielding deoxycholic acid and lithocholic acid, respectively. Highest affinity with taurochenodeoxycholic acid.  
[https://www.uniprot.org/uniprot/BAIA2_CLOSV BAIA2_CLOSV] Involved in the multi-step bile acid 7alpha-dehydroxylation pathway that transforms primary bile acids to secondary bile acids in the human gut (PubMed:16299351, PubMed:23836456). Catalyzes the oxidation of C3-hydroxyl group of CoA conjugated bile acids generating a C3-oxo bile acid intermediate. Can use choloyl-CoA, chenodeoxycholoyl-CoA, deoxycholoyl-CoA, and lithocholoyl-CoA as substrates with similar efficiency. Highly prefers NAD over NADP as cosubstrate. Also catalyzes the reverse reactions; in vitro, the preferred direction of reaction depends on the pH. Has very little activity with unconjugated (non-CoA) bile acid substrates (PubMed:23836456).<ref>PMID:23836456</ref> <ref>PMID:16299351</ref>
 
==See Also==
*[[Hydroxysteroid dehydrogenase 3D structures|Hydroxysteroid dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 35704]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Jcsg]]
[[Category: Oxidoreductase]]
[[Category: PSI, Protein structure initiative]]
[[Category: Psi-biology]]

Latest revision as of 10:03, 27 November 2024

Crystal structure of a 3alpha-hydroxysteroid dehydrogenase (BaiA2) associated with secondary bile acid synthesis from Clostridium scindens VPI12708 in complex with a putative NAD(+)-OH- adduct at 2.0 A resolutionCrystal structure of a 3alpha-hydroxysteroid dehydrogenase (BaiA2) associated with secondary bile acid synthesis from Clostridium scindens VPI12708 in complex with a putative NAD(+)-OH- adduct at 2.0 A resolution

Structural highlights

4is3 is a 4 chain structure with sequence from Clostridium scindens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BAIA2_CLOSV Involved in the multi-step bile acid 7alpha-dehydroxylation pathway that transforms primary bile acids to secondary bile acids in the human gut (PubMed:16299351, PubMed:23836456). Catalyzes the oxidation of C3-hydroxyl group of CoA conjugated bile acids generating a C3-oxo bile acid intermediate. Can use choloyl-CoA, chenodeoxycholoyl-CoA, deoxycholoyl-CoA, and lithocholoyl-CoA as substrates with similar efficiency. Highly prefers NAD over NADP as cosubstrate. Also catalyzes the reverse reactions; in vitro, the preferred direction of reaction depends on the pH. Has very little activity with unconjugated (non-CoA) bile acid substrates (PubMed:23836456).[1] [2]

See Also

References

  1. ↑ Bhowmik S, Jones DH, Chiu HP, Park IH, Chiu HJ, Axelrod HL, Farr CL, Tien HJ, Agarwalla S, Lesley SA. Structural and functional characterization of BaiA, an enzyme involved in secondary bile acid synthesis in human gut microbe. Proteins. 2014 Feb;82(2):216-29. doi: 10.1002/prot.24353. Epub 2013 Oct 17. PMID:23836456 doi:http://dx.doi.org/10.1002/prot.24353
  2. ↑ Ridlon JM, Kang DJ, Hylemon PB. Bile salt biotransformations by human intestinal bacteria. J Lipid Res. 2006 Feb;47(2):241-59. doi: 10.1194/jlr.R500013-JLR200. Epub 2005, Nov 18. PMID:16299351 doi:http://dx.doi.org/10.1194/jlr.R500013-JLR200

4is3, resolution 2.00Å

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