3SLK
Structure of ketoreductase and enoylreductase didomain from modular polyketide synthase
Summary for 3SLK
| Entry DOI | 10.2210/pdb3slk/pdb |
| Descriptor | Polyketide synthase extender module 2, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION (3 entities in total) |
| Functional Keywords | rossmann fold, nadph, oxidoreductase |
| Biological source | Saccharopolyspora spinosa |
| Total number of polymer chains | 2 |
| Total formula weight | 170118.98 |
| Authors | Zheng, J.,Gay, D.C.,Keatinge-Clay, A.T. (deposition date: 2011-06-24, release date: 2012-05-30, Last modification date: 2024-02-28) |
| Primary citation | Zheng, J.,Gay, D.C.,Demeler, B.,White, M.A.,Keatinge-Clay, A.T. Divergence of multimodular polyketide synthases revealed by a didomain structure. Nat.Chem.Biol., 8:615-621, 2012 Cited by PubMed Abstract: The enoylreductase (ER) is the final common enzyme from modular polyketide synthases (PKSs) to be structurally characterized. The 3.0 Å-resolution structure of the didomain comprising the ketoreductase (KR) and ER from the second module of the spinosyn PKS reveals that ER shares an ∼600-Å(2) interface with KR distinct from that of the related mammalian fatty acid synthase (FAS). In contrast to the ER domains of the mammalian FAS, the ER domains of the second module of the spinosyn PKS do not make contact across the two-fold axis of the synthase. This monomeric organization may have been necessary in the evolution of multimodular PKSs to enable acyl carrier proteins to access each of their cognate enzymes. The isolated ER domain showed activity toward a substrate analog, enabling us to determine the contributions of its active site residues. PubMed: 22634636DOI: 10.1038/nchembio.964 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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