4WAS
STRUCTURE OF THE ETR1P/NADP/CROTONYL-COA COMPLEX
Summary for 4WAS
| Entry DOI | 10.2210/pdb4was/pdb |
| Related | 4W99 |
| Descriptor | Enoyl-[acyl-carrier-protein] reductase [NADPH, B-specific] 1, mitochondrial, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, CROTONYL COENZYME A, ... (4 entities in total) |
| Functional Keywords | mitochondrial fatty acid synthesis, oxidoreductase |
| Biological source | Candida tropicalis (Yeast) |
| Cellular location | Mitochondrion : Q8WZM3 |
| Total number of polymer chains | 3 |
| Total formula weight | 123403.24 |
| Authors | Quade, N.,Voegeli, B.,Rosenthal, R.,Capitani, G.,Erb, T.J. (deposition date: 2014-08-31, release date: 2015-03-18, Last modification date: 2024-01-10) |
| Primary citation | Rosenthal, R.G.,Vogeli, B.,Quade, N.,Capitani, G.,Kiefer, P.,Vorholt, J.A.,Ebert, M.O.,Erb, T.J. The use of ene adducts to study and engineer enoyl-thioester reductases. Nat.Chem.Biol., 11:398-400, 2015 Cited by PubMed Abstract: 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. PubMed: 25867044DOI: 10.1038/nchembio.1794 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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