4DBZ
Crystal Structure of V151L Actinorhodin Polyketide Ketoreductase with NADPH
Summary for 4DBZ
| Entry DOI | 10.2210/pdb4dbz/pdb |
| Related | 4DC0 4DC1 |
| Descriptor | Ketoacyl reductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | rossmann fold, ketoreductase, oxidoreductase |
| Biological source | Streptomyces coelicolor |
| Total number of polymer chains | 2 |
| Total formula weight | 60447.62 |
| Authors | Javidpour, P.,Tsai, S.-C. (deposition date: 2012-01-16, release date: 2013-01-16, Last modification date: 2024-02-28) |
| Primary citation | Javidpour, P.,Bruegger, J.,Srithahan, S.,Korman, T.P.,Crump, M.P.,Crosby, J.,Burkart, M.D.,Tsai, S.C. The Determinants of Activity and Specificity in Actinorhodin Type II Polyketide Ketoreductase. Chem.Biol., 20:1225-1234, 2013 Cited by PubMed Abstract: In the actinorhodin type II polyketide synthase, the first polyketide modification is a regiospecific C9-carbonyl reduction, catalyzed by the ketoreductase (actKR). Our previous studies identified the actKR 94-PGG-96 motif as a determinant of stereospecificity. The molecular basis for reduction regiospecificity is, however, not well understood. In this study, we examined the activities of 20 actKR mutants through a combination of kinetic studies, PKS reconstitution, and structural analyses. Residues have been identified that are necessary for substrate interaction, and these observations have suggested a structural model for this reaction. Polyketides dock at the KR surface and are steered into the enzyme pocket where C7-C12 cyclization is mediated by the KR before C9-ketoreduction can occur. These molecular features can potentially serve as engineering targets for the biosynthesis of novel, reduced polyketides. PubMed: 24035284DOI: 10.1016/j.chembiol.2013.07.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.643 Å) |
Structure validation
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