4A0S
STRUCTURE OF THE 2-OCTENOYL-COA CARBOXYLASE REDUCTASE CINF IN COMPLEX WITH NADP AND 2-OCTENOYL-COA
Summary for 4A0S
| Entry DOI | 10.2210/pdb4a0s/pdb |
| Related | 4A10 |
| Descriptor | OCTENOYL-COA REDUCTASE/CARBOXYLASE, OCTANOYL-COENZYME A, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, transferase, cinnabaramide pks biosynthesis |
| Biological source | STREPTOMYCES SP. |
| Total number of polymer chains | 4 |
| Total formula weight | 198670.62 |
| Authors | Quade, N.,Huo, L.,Rachid, S.,Heinz, D.W.,Muller, R. (deposition date: 2011-09-12, release date: 2011-12-07, Last modification date: 2023-12-20) |
| Primary citation | Quade, N.,Huo, L.,Rachid, S.,Heinz, D.W.,Muller, R. Unusual carbon fixation gives rise to diverse polyketide extender units. Nat. Chem. Biol., 8:117-124, 2011 Cited by PubMed Abstract: Polyketides are structurally diverse and medically important natural products that have various biological activities. During biosynthesis, chain elongation uses activated dicarboxylic acid building blocks, and their availability therefore limits side chain variation in polyketides. Recently, the crotonyl-CoA carboxylase-reductase (CCR) class of enzymes was identified in primary metabolism and was found to be involved in extender-unit biosynthesis of polyketides. These enzymes are, in theory, capable of forming dicarboxylic acids that show any side chain from the respective unsaturated fatty acid precursor. To our knowledge, we here report the first crystal structure of a CCR, the hexylmalonyl-CoA synthase from Streptomyces sp. JS360, in complex with its substrate. Structural analysis and biochemical characterization of the enzyme, including active site mutations, are reported. Our analysis reveals how primary metabolic CCRs can evolve to produce various dicarboxylic acid building blocks, setting the stage to use CCRs for the production of unique extender units and, consequently, altered polyketides. PubMed: 22138621DOI: 10.1038/nchembio.734 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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