8wbq | pdb_00008wbq

Crystal structure of cis-Epoxysuccinate Hydrolases RhCESH[L] mutant E212Q complexed with L-TA.

spinqualitylabelsall models 8wbq, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8wbq is a 2 chain structure with sequence from Rhodococcus opacus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: TLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q1KLR5_RHOOP 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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