4a10

Apo-structure of 2-octenoyl-CoA carboxylase reductase CinF from streptomyces sp.

spinqualitylabelsall models 4a10, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4a10 is a 4 chain structure with sequence from Streptomyces cinnabarigriseus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F0V3Z3_9ACTN Publication Abstract from PubMed 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. Unusual carbon fixation gives rise to diverse polyketide extender units.,Quade N, Huo L, Rachid S, Heinz DW, Muller R Nat Chem Biol. 2011 Dec 4;8(1):117-24. doi: 10.1038/nchembio.734. PMID:22138621 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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