8wmt: Difference between revisions
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==Crystal structure of cis-epoxysuccinic hydrolase from Bradyrhizobium mercantei== | |||
<StructureSection load='8wmt' size='340' side='right'caption='[[8wmt]], [[Resolution|resolution]] 1.72Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8wmt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_mercantei Bradyrhizobium mercantei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WMT 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]] 1.72Å</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=8wmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wmt OCA], [https://pdbe.org/8wmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wmt RCSB], [https://www.ebi.ac.uk/pdbsum/8wmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wmt ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
l-(+)-Tartaric acid plays important roles in various industries, including pharmaceuticals, foods, and chemicals. cis-Epoxysuccinate hydrolases (CESHs) are crucial for converting cis-epoxysuccinate to l-(+)-tartrate in the industrial production process. There is, however, a lack of detailed structural and mechanistic information on CESHs, limiting the discovery and engineering of these industrially relevant enzymes. In this study, we report the crystal structures of RoCESH and KoCESH-l-(+)-tartrate complex. These structures reveal the key amino acids of the active pocket and the catalytic triad residues and elucidate a dynamic catalytic process involving conformational changes of the active site. Leveraging the structural insights, we identified a robust BmCESH (550 +/- 20 U.mg(-1)) with sustained catalytic activity even at a 3 M substrate concentration. After six batches of transformation, immobilized cells with overexpressed BmCESH maintained 69% of their initial activity, affording an overall productivity of 200 g/L/h. These results provide valuable insights into the development of high-efficiency CESHs and the optimization of biotransformation processes for industrial uses. | |||
Structural Insights of a cis-Epoxysuccinate Hydrolase Facilitate the Development of Robust Biocatalysts for the Production of l-(+)-Tartrate.,Han Y, Luo Y, Ma BD, Li J, Xu JH, Kong XD Biochemistry. 2024 May 27. doi: 10.1021/acs.biochem.4c00141. PMID:38803051<ref>PMID:38803051</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8wmt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bradyrhizobium mercantei]] | |||
[[Category: Large Structures]] | |||
[[Category: Han Y]] | |||
[[Category: Kong XD]] | |||
[[Category: Xu JH]] | |||
Latest revision as of 05:06, 12 June 2024
Crystal structure of cis-epoxysuccinic hydrolase from Bradyrhizobium mercantei
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