8wbl: Difference between revisions
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==Crystal structure of cis-Epoxysuccinate Hydrolases RhCESH[L] complexed with sulfate ions== | |||
<StructureSection load='8wbl' size='340' side='right'caption='[[8wbl]], [[Resolution|resolution]] 1.94Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8wbl]] 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=8WBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WBL FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.941Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8wbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wbl OCA], [https://pdbe.org/8wbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wbl RCSB], [https://www.ebi.ac.uk/pdbsum/8wbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wbl ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q1KLR5_RHOOP Q1KLR5_RHOOP] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8wbl" style="background-color:#fffaf0;"></div> | ||
[[Category: Cui | == References == | ||
[[Category: | <references/> | ||
[[Category: Feng | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rhodococcus opacus]] | |||
[[Category: Cui Q]] | |||
[[Category: Dong S]] | |||
[[Category: Feng YG]] | |||
[[Category: Xuan JS]] | |||