6iyt

Crystal Structure of the acyltransferase domain from second module 14 of salinomycin polyketide synthase

spinqualitylabelsall models 6iyt, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6iyt is a 2 chain structure with sequence from Streptomyces albus subsp. albus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.78Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H1ZZU1_9ACTN Publication Abstract from PubMed Salinomycin with antibacterial and anticoccidial activities is a commercial polyether polyketide widely used in animal husbandry as a food additive. Malonyl-CoA (MCoA), methylmalonyl-CoA (MMCoA), and ethylmalonyl-CoA (EMCoA) are used as extension units in its biosynthesis. To understand how the salinomycin modular polyketide synthase (PKS) strictly discriminates among these extension units, the acyltransferase (AT) domains selecting MCoA, MMCoA, and EMCoA were structurally characterized. Molecular dynamics simulations of the AT structures helped to reveal the key interactions involved in enzyme-substrate recognitions, which enabled the engineering of AT mutants with switched specificity. The catalytic efficiencies ( kcat/ Km) of these AT mutants are comparable with those of the wild-type AT domains. These results set the stage for engineering the AT substrate specificity of modular PKSs. Structural Insights into the Substrate Specificity of Acyltransferases from Salinomycin Polyketide Synthase.,Zhang F, Shi T, Ji H, Ali I, Huang S, Deng Z, Min Q, Bai L, Zhao Y, Zheng J Biochemistry. 2019 Jun 19. doi: 10.1021/acs.biochem.9b00305. PMID:31199122 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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