4was | pdb_00004was

STRUCTURE OF THE ETR1P/NADP/CROTONYL-COA COMPLEX

spinqualitylabelsall models 4was, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4was is a 3 chain structure with sequence from Candida tropicalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: COO, NAP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ETR1_CANTR Required for respiration and the maintenance of the mitochondrial compartment. May have a role in the mitochondrial synthesis of fatty acids. Publication Abstract from PubMed An improved understanding of enzymes' catalytic proficiency and stereoselectivity would further enable applications in chemistry, biocatalysis and industrial biotechnology. We use a chemical probe to dissect individual catalytic steps of enoyl-thioester reductases (Etrs), validating an active site tyrosine as the cryptic proton donor and explaining how it had eluded definitive identification. This information enabled the rational redesign of Etr, yielding mutants that create products with inverted stereochemistry at wild type-like turnover frequency. The use of ene adducts to study and engineer enoyl-thioester reductases.,Rosenthal RG, Vogeli B, Quade N, Capitani G, Kiefer P, Vorholt JA, Ebert MO, Erb TJ Nat Chem Biol. 2015 Apr 13. doi: 10.1038/nchembio.1794. PMID:25867044 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Enoyl-Acyl-Carrier Protein Reductase 3D structures

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