6kxd

The ishigamide ketosynthase/chain length factor

spinqualitylabelsall models 6kxd, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6kxd is a 2 chain structure with sequence from Streptomyces sp. MSC090213JE08. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: ACT, EDO, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1Y1BW67_9ACTN Publication Abstract from PubMed In type II polyketide synthases (PKSs), the ketosynthase-chain length factor (KS-CLF) complex catalyzes polyketide chain elongation with the acyl carrier protein (ACP). Highly reducing type II PKSs, represented by IgaPKS, produce polyene structures instead of the well-known aromatic skeletons. Here, we report the crystal structures of the Iga11-Iga12 (KS-CLF) heterodimer and the covalently cross-linked Iga10=Iga11-Iga12 (ACP=KS-CLF) tripartite complex. The latter structure revealed the molecular basis of the interaction between Iga10 and Iga11-Iga12, which differs from that between the ACP and KS of Escherichia coli fatty acid synthase. Furthermore, the reaction pocket structure and site-directed mutagenesis revealed that the negative charge of Asp 113 of Iga11 prevents further condensation using a beta-ketoacyl product as a substrate, which distinguishes IgaPKS from typical type II PKSs. This work will facilitate the future rational design of PKSs. Structural basis for selectivity in a highly reducing type II polyketide synthase.,Du D, Katsuyama Y, Horiuchi M, Fushinobu S, Chen A, Davis TD, Burkart MD, Ohnishi Y Nat Chem Biol. 2020 May 4. pii: 10.1038/s41589-020-0530-0. doi:, 10.1038/s41589-020-0530-0. PMID:32367018 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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