5ydl | pdb_00005ydl

The crystal structure of the Acyl Transferase domain of SpnD complex with 2-(pent-4-yn-1-yl)malonyl

spinqualitylabelsall models 5ydl, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ydl is a 1 chain structure with sequence from Streptomyces sp. CNQ431. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.402Å Ligands: DUV Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0E3JLZ0_9ACTN Publication Abstract from PubMed Polyketides are a large family of pharmaceutically important natural products, and the structural modification of their scaffolds is significant for drug development. Herein, we report high-resolution X-ray crystal structures of the broadly selective acyltransferase (AT) from the splenocin polyketide synthase (SpnD-AT) in the apo form and in complex with benzylmalonyl and pentynylmalonyl extender unit mimics. These structures revealed the molecular basis for the stereoselectivity and substrate specificity of SpnD-AT, and enabled the engineering of the industrially important Ery-AT6 to broaden its substrate scope to include three new types of extender units. Structural Basis of a Broadly Selective Acyltransferase from the Polyketide Synthase of Splenocin.,Li Y, Zhang W, Zhang H, Tian W, Wu L, Wang S, Zheng M, Zhang J, Sun C, Deng Z, Sun Y, Qu X, Zhou J Angew Chem Int Ed Engl. 2018 May 14;57(20):5823-5827. doi:, 10.1002/anie.201802805. Epub 2018 Apr 14. PMID:29536601 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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