4gh5

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==Crystal structure of S-2-hydroxypropyl coenzyme M dehydrogenase (S-HPCDH)==
==Crystal structure of S-2-hydroxypropyl coenzyme M dehydrogenase (S-HPCDH)==
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<StructureSection load='4gh5' size='340' side='right' caption='[[4gh5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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<StructureSection load='4gh5' size='340' side='right'caption='[[4gh5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4gh5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanp2 Xanp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GH5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GH5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4gh5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthobacter_autotrophicus_Py2 Xanthobacter autotrophicus Py2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GH5 FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Xaut_5073 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=78245 XANP2])</td></tr>
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<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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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<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=4gh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gh5 OCA], [http://pdbe.org/4gh5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gh5 RCSB], [http://www.ebi.ac.uk/pdbsum/4gh5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gh5 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gh5 OCA], [https://pdbe.org/4gh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gh5 RCSB], [https://www.ebi.ac.uk/pdbsum/4gh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gh5 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/HCDS3_XANP2 HCDS3_XANP2] Involved in aliphatic epoxide carboxylation (PubMed:20302306). Catalyzes the reversible oxidation of (2S)-2-hydroxypropyl-coenzyme M (S-HPC) to 2-oxopropyl-coenzyme M (2-KPC) (PubMed:20302306). The enzyme is highly specific for the S enantiomers (PubMed:20302306). In vitro can also use the aliphatic ketone 2-butanone and the aliphatic alcohol 2-propanol, and shows an inherent stereoselectivity for 2-butanone reduction (PubMed:20302306).<ref>PMID:20302306</ref>
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(R)- and (S)-hydroxypropyl-coenzyme M dehydrogenases (R- and S-HPCDH) are stereospecific enzymes that are central to the metabolism of propylene and epoxide in Xanthobacter autotrophicus. The bacterium produces R- and S-HPCDH simultaneously to facilitate transformation of R- and S-enantiomers of epoxypropane to a common achiral product 2-ketopropyl-CoM (2-KPC). Both R- and S-HPCDH are highly specific for their respective substrates as each enzyme displays less than 0.5% activity with the opposite substrate isomer. In order to elucidate the structural basis for stereospecificity displayed by R- and S-HPCDH we have determined substrate bound crystal structures of S-HPCDH to 1.6A resolution. Comparisons to the previously reported product-bound structure of R-HPCDH reveal that although the placement of catalytic residues within the active site of each enzyme is nearly identical, structural differences in the surrounding area provide each enzyme with a distinct substrate binding pocket. These structures demonstrate how chiral discrimination by R- and S-HPCDH results from alternative binding of the distal end of substrates within each substrate binding pocket.
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Crystal structures of S-HPCDH reveal determinants of stereospecificity for R- and S-hydroxypropyl-coenzyme M dehydrogenases.,Bakelar JW, Sliwa DA, Johnson SJ Arch Biochem Biophys. 2013 Mar 6. pii: S0003-9861(13)00068-4. doi:, 10.1016/j.abb.2013.02.017. PMID:23474457<ref>PMID:23474457</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4gh5" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Xanp2]]
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[[Category: Large Structures]]
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[[Category: Bakelar, J W]]
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[[Category: Xanthobacter autotrophicus Py2]]
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[[Category: Johnson, S J]]
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[[Category: Bakelar JW]]
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[[Category: Oxidoreductase]]
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[[Category: Johnson SJ]]
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[[Category: Rossmann fold]]
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Current revision

Crystal structure of S-2-hydroxypropyl coenzyme M dehydrogenase (S-HPCDH)

PDB ID 4gh5

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