3slk | pdb_00003slk

Structure of ketoreductase and enoylreductase didomain from modular polyketide synthase

spinqualitylabelsall models 3slk, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3slk is a 2 chain structure with sequence from Atcc 49460. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NDP, SO4 Gene: spnB (ATCC 49460) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The enoylreductase (ER) is the final common enzyme from modular polyketide synthases (PKSs) to be structurally characterized. The 3.0 A-resolution structure of the didomain comprising the ketoreductase (KR) and ER from the second module of the spinosyn PKS reveals that ER shares an approximately 600-A(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. Divergence of multimodular polyketide synthases revealed by a didomain structure.,Zheng J, Gay DC, Demeler B, White MA, Keatinge-Clay AT Nat Chem Biol. 2012 May 27. doi: 10.1038/nchembio.964. PMID:22634636 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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