4ftw | pdb_00004ftw

Crystal structure of a carboxyl esterase N110C/L145H at 2.3 angstrom resolution

spinqualitylabelsall models 4ftw, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ftw is a 1 chain structure with sequence from Cereibacter sphaeroides 2.4.1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: 3CM, CL, NA, PIN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3J2V1_CERS4 Publication Abstract from PubMed The present work created an esterase variant from Rhodobacter sphaeroides (RspE) with enhanced selectivity in hydrolytic kinetic resolutions by directed evolution. A "model" substrate, methyl mandelate, was introduced in the high-throughput screening procedure. E values of a variant CH (Asn62Cys/Leu145His) for six different esters were 10-83, which were a relative improvement compared to 2-20 for the wild type. Our subsequent crystal structure interpretation and molecular dynamics simulations helped shed light on the source of enantioselectivity modified by directed evolution. Though mutations displayed no "direct" interaction with the substrate, they were hypothesized to strengthen the intramolecular interaction in the catalytic cavity of variant. Conformation analysis revealed that the enhanced enantioselectivity of variant CH for the seven substrates applied in this study was derived from the decrease in size of the substrate binding pocket. Enhanced enantioselectivity of a carboxyl esterase from Rhodobacter sphaeroides by directed evolution.,Ma J, Wu L, Guo F, Gu J, Tang X, Jiang L, Liu J, Zhou J, Yu H Appl Microbiol Biotechnol. 2012 Sep 19. PMID:22987200 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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