4gh5: Difference between revisions

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'''Unreleased structure'''


The entry 4gh5 is ON HOLD
==Crystal structure of S-2-hydroxypropyl coenzyme M dehydrogenase (S-HPCDH)==
 
<StructureSection load='4gh5' size='340' side='right'caption='[[4gh5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
Authors: Bakelar, J.W., Johnson, S.J.
== 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>
Description: Crystal structure of S-2-hydroxypropyl coenzyme M dehydrogenase (S-HPCDH)
</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>
</table>
== 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>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xanthobacter autotrophicus Py2]]
[[Category: Bakelar JW]]
[[Category: Johnson SJ]]

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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