8wbt | pdb_00008wbt

Crystal structure of cis-Epoxysuccinate Hydrolases KlCESH[L] mutant D48N complexed with L-TA

spinqualitylabelsall models 8wbt, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8wbt is a 4 chain structure with sequence from Klebsiella sp. BK-58. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: CA, GOL, TLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W8PFD2_KLEOX Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids.[RuleBase:RU368077] 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 Jan 8:105635. doi: 10.1016/j.jbc.2024.105635. PMID:38199576 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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