2cfc

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{{Seed}}
 
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[[Image:2cfc.png|left|200px]]
 
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==structural basis for stereo selectivity in the (R)- and (S)- hydroxypropylethane thiosulfonate dehydrogenases==
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The line below this paragraph, containing "STRUCTURE_2cfc", creates the "Structure Box" on the page.
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<StructureSection load='2cfc' size='340' side='right'caption='[[2cfc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2cfc]] 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=2CFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CFC FirstGlance]. <br>
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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]] 1.8&#8491;</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=KPC:(2-[2-KETOPROPYLTHIO]ETHANESULFONATE'>KPC</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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{{STRUCTURE_2cfc| PDB=2cfc | SCENE= }}
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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=2cfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfc OCA], [https://pdbe.org/2cfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cfc RCSB], [https://www.ebi.ac.uk/pdbsum/2cfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cfc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HCDR1_XANP2 HCDR1_XANP2] Involved in aliphatic epoxide carboxylation (PubMed:9405410, PubMed:10411892, PubMed:11851420). Catalyzes the reversible oxidation of (R)-2-hydroxypropyl-coenzyme M (R-HPC) to 2-oxopropyl-coenzyme M (2-KPC) (PubMed:10411892, PubMed:11851420, PubMed:15157110, PubMed:20302306). The enzyme is highly specific for the R enantiomers (PubMed:10411892, PubMed:15157110, PubMed:20302306). In vitro can also use achiral 2-propanol and short-chain (R)- and (S)-2-alkanols (PubMed:15157110).<ref>PMID:10411892</ref> <ref>PMID:11851420</ref> <ref>PMID:15157110</ref> <ref>PMID:20302306</ref> <ref>PMID:9405410</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/2cfc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cfc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Epoxide metabolism in Xanthobacter autotrophicus Py2 results in the conversion of epoxypropane to acetoacetate. Epoxide metabolism is initiated by the nucleophilic addition of coenzyme M to the (R)- and (S)-enantiomers of epoxypropane which forms the respective enantiomers of 2-hydroxypropyl-coenyme M. The (R)- and (S)-enantiomers of 2-hydroxypropyl coenzyme are oxidized to the achiral product 2-ketopropyl-CoM by two stereoselective dehydrogenases. The dehydrogenases catalyzing these reactions, termed (R)-hydroxypropyl-coenzyme M dehydrogenase (R-HPCDH) and (S)-hydroxypropyl-coenzyme M dehydrogenase (S-HPCDH), are NAD(+)-dependent enzymes belonging to the short chain dehydrogenase/reductase (SDR) family of enzymes. In this study, the crystal structure of R-HPCDH cocrystallized in the presence of (S)-hydroxypropyl-coenzyme M has been determined using X-ray diffraction methods and refined to 1.8 A resolution. The structure of R-HPCDH is tetrameric and stabilized by the interaction of the terminal carboxylates of each subunit with divalent metal ions. The structure of the presumed product-bound state reveals that binding interactions between the negatively charged oxygen atoms of the sulfonate moiety have striking similarities to sulfonate interactions observed in the previously determined structure of 2-ketopropyl-CoM oxidoreductase/carboxylase, highlighting the utility of coenzyme M as a carrier molecule in the pathway. The key elements of the aforementioned interactions are electrostatic interactions between the sulfonate oxygen atoms and two arginine residues (R152 and R196) of R-HPCDH. The comparison of the structure of R-HPCDH with a homology model of S-HPCDH provides a structural basis for a mechanism of substrate specificity in which the binding of the substrate sulfonate moiety at distinct sites on each stereoselective enzyme directs the orientation of the appropriate substrate enantiomer for hydride abstraction.
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===STRUCTURAL BASIS FOR STEREO SELECTIVITY IN THE (R)- AND (S)-HYDROXYPROPYLETHANE THIOSULFONATE DEHYDROGENASES===
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Structural basis for stereoselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases.,Krishnakumar AM, Nocek BP, Clark DD, Ensign SA, Peters JW Biochemistry. 2006 Jul 25;45(29):8831-40. PMID:16846226<ref>PMID:16846226</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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The line below this paragraph, {{ABSTRACT_PUBMED_16846226}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2cfc" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16846226 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16846226}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2CFC is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFC OCA].
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[[Category: Xanthobacter autotrophicus Py2]]
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[[Category: Clark DD]]
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==Reference==
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[[Category: Ensign SA]]
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<ref group="xtra">PMID:16846226</ref><references group="xtra"/>
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[[Category: Krishnakumar AM]]
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[[Category: Xanthobacter autotrophicus]]
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[[Category: Nocek BP]]
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[[Category: Clark, D D.]]
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[[Category: Peters JW]]
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[[Category: Ensign, S A.]]
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[[Category: Krishnakumar, A M.]]
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[[Category: Nocek, B P.]]
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[[Category: Peters, J W.]]
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[[Category: Nad]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 16:52:06 2009''
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Current revision

structural basis for stereo selectivity in the (R)- and (S)- hydroxypropylethane thiosulfonate dehydrogenases

PDB ID 2cfc

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