5b00

Structure of the prenyltransferase MoeN5 in complex with geranyl pyrophosphate

spinqualitylabelsall models 5b00, resolution 2.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5b00 is a 3 chain structure with sequence from Streptomyces viridosporus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GPP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A010_STRVD Publication Abstract from PubMed The structure of MoeN5, a unique prenyltransferase involved in the biosynthesis of the antibiotic moenomycin, is reported. MoeN5 catalyzes the reaction of geranyl diphosphate (GPP) with the cis-farnesyl group in phosphoglycolipid 5 to form the (C25 ) moenocinyl-sidechain-containing lipid 7. GPP binds to an allylic site (S1) and aligns well with known S1 inhibitors. Alkyl glycosides, glycolipids, can bind to both S1 and a second site, S2. Long sidechains in S2 are "bent" and co-locate with the homoallylic substrate isopentenyl diphosphate in other prenyltransferases. These observations support a MoeN5 mechanism in which 5 binds to S2 with its C6-C11 group poised to attack C1 in GPP to form the moenocinyl sidechain, with the more distal regions of 5 aligning with the distal glucose in decyl maltoside. The results are of general interest because they provide the first structures of MoeN5 and a structural basis for its mechanism of action, results that will facilitate the design of new antibiotics. Moenomycin Biosynthesis: Structure and Mechanism of Action of the Prenyltransferase MoeN5.,Zhang L, Chen CC, Ko TP, Huang JW, Zheng Y, Liu W, Wang I, Malwal SR, Feng X, Wang K, Huang CH, Hsu ST, Wang AH, Oldfield E, Guo RT Angew Chem Int Ed Engl. 2016 Apr 4;55(15):4716-20. doi: 10.1002/anie.201511388., Epub 2016 Mar 8. PMID:26954060 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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