5xk7

Crystal structure of Isosesquilavandulyl Diphosphate Synthase from Streptomyces sp. strain CNH-189 in complex with DMAPP

spinqualitylabelsall models 5xk7, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xk7 is a 4 chain structure with sequence from Streptomyces sp. CNH189. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.911Å Ligands: DMA, MES, MG, POP, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M4T4U9_9ACTN Publication Abstract from PubMed We report the first X-ray crystallographic structure of the "head-to-middle" prenyltransferase, isosesquilavandulyl diphosphate synthase, involved in biosynthesis of the merochlorin class of antibiotics. The protein adopts the zeta or cis-prenyl transferase fold but remarkably, unlike tuberculosinol adenosine synthase and other cis-prenyl transferases (e.g. cis-farnesyl, decaprenyl, undecaprenyl diphosphate synthases), the large, hydrophobic side chain does not occupy a central hydrophobic tunnel. Instead, it occupies a surface pocket oriented at 90 degrees to the hydrophobic tunnel. Product chain-length control is achieved by squeezing out the ligand from the conventional allylic S1 binding site, with proton abstraction being achieved using a diphosphate-Asn-Ser relay. The structures revise and unify our thinking as to the mechanism of action of many other prenyl transferases and may also be of use in engineering new merochlorin-class antibiotics. "Head-to-Middle" and "Head-to-Tail" cis-Prenyl Transferases: Structure of Isosesquilavandulyl Diphosphate Synthase.,Gao J, Ko TP, Chen L, Malwal SR, Zhang J, Hu X, Qu F, Liu W, Huang JW, Cheng YS, Chen CC, Yang Y, Zhang Y, Oldfield E, Guo RT Angew Chem Int Ed Engl. 2018 Jan 15;57(3):683-687. doi: 10.1002/anie.201710185., Epub 2017 Dec 21. PMID:29215779 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Undecaprenyl pyrophosphate synthase

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