4gh5: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<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>
<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>
</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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 1.6&#8491;</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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=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>
<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>
== Function ==
== Function ==
[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>  
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
(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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4gh5" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 18:46, 14 March 2024

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

Structural highlights

4gh5 is a 4 chain structure with sequence from Xanthobacter autotrophicus Py2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1]

References

  1. ↑ Sliwa DA, Krishnakumar AM, Peters JW, Ensign SA. Molecular basis for enantioselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases, a unique pair of stereoselective short-chain dehydrogenases/reductases involved in aliphatic epoxide carboxylation. Biochemistry. 2010 Apr 27;49(16):3487-98. doi: 10.1021/bi100294m. PMID:20302306 doi:http://dx.doi.org/10.1021/bi100294m

4gh5, resolution 1.60Å

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