2d52

Pentaketide chromone synthase (M207G mutant complexed with Coa)

spinqualitylabelsall models 2d52, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2d52 is a 2 chain structure with sequence from Aloar. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: COA NonStd Res: CSD Related: 2d3m, 1bq6, 1ee0, 2d51 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PCS_ALOAR] Catalyzes the iterative condensations of 5 molecules of malonyl-CoA to produce a pentaketide 5,7-dihydroxy-2-methylchromone. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structures of a wild-type and a mutant PCS, a novel plant type III polyketide synthase from a medicinal plant, Aloe arborescens, were solved at 1.6 A resolution. The crystal structures revealed that the pentaketide-producing wild-type and the octaketide-producing M207G mutant shared almost the same overall folding, and that the large-to-small substitution dramatically increases the volume of the polyketide-elongation tunnel by opening a gate to two hidden pockets behind the active site of the enzyme. The chemically inert active site residue 207 thus controls the number of condensations of malonyl-CoA, solely depending on the steric bulk of the side chain. These findings not only provided insight into the polyketide formation reaction, but they also suggested strategies for the engineered biosynthesis of polyketides. Structural insight into chain-length control and product specificity of pentaketide chromone synthase from Aloe arborescens.,Morita H, Kondo S, Oguro S, Noguchi H, Sugio S, Abe I, Kohno T Chem Biol. 2007 Apr;14(4):359-69. PMID:17462571 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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