8wbp

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'''Unreleased structure'''
 
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The entry 8wbp is ON HOLD
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==Crystal structure of cis-Epoxysuccinate Hydrolases RhCESH[L] mutant E212Q==
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<StructureSection load='8wbp' size='340' side='right'caption='[[8wbp]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8wbp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WBP 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]] 1.87&#8491;</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=8wbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wbp OCA], [https://pdbe.org/8wbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wbp RCSB], [https://www.ebi.ac.uk/pdbsum/8wbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wbp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q1KLR5_RHOOP Q1KLR5_RHOOP]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Microbial epoxide hydrolases, cis-epoxysuccinate hydrolases (CESHs), have been utilized for commercial production of enantiomerically pure L(+)- and D(-)-tartaric acids for decades. However, the stereo-catalytic mechanism of CESH producing L(+)-tartaric acid (CESH[L]) remains unclear. Herein, the crystal structures of two CESH[L]s in ligand-free, product-complexed, and catalytic intermediate forms were determined. These structures revealed the unique specific binding mode for the mirror-symmetric substrate, an active catalytic triad consisting of Asp-His-Glu, and an arginine providing a proton to the oxirane oxygen to facilitate the epoxide ring-opening reaction, which has been pursued for decades. These results provide the structural basis for the rational engineering of these industrial biocatalysts.
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Authors: Dong, S., Xuan, J.S., Feng, Y.G., Cui, Q.
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Deciphering the stereo-specific catalytic mechanisms of cis-epoxysuccinate hydrolases producing L(+)-tartaric acid.,Dong S, Xuan J, Feng Y, Cui Q J Biol Chem. 2024 Feb;300(2):105635. doi: 10.1016/j.jbc.2024.105635. Epub 2024 , Jan 8. PMID:38199576<ref>PMID:38199576</ref>
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Description: Crystal structure of cis-Epoxysuccinate Hydrolases RhCESH[L] mutant E212Q
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Dong, S]]
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<div class="pdbe-citations 8wbp" style="background-color:#fffaf0;"></div>
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[[Category: Xuan, J.S]]
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== References ==
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[[Category: Cui, Q]]
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<references/>
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[[Category: Feng, Y.G]]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Rhodococcus opacus]]
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[[Category: Cui Q]]
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[[Category: Dong S]]
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[[Category: Feng YG]]
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[[Category: Xuan JS]]

Current revision

Crystal structure of cis-Epoxysuccinate Hydrolases RhCESH[L] mutant E212Q

PDB ID 8wbp

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