4yla

Crystal structure of the indole prenyltransferase MpnD complexed with indolactam V and DMSPP

spinqualitylabelsall models 4yla, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4yla is a 1 chain structure with sequence from Marinactinospora thermotolerans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: DST, ILV, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I7EIW6_9ACTN Publication Abstract from PubMed Prenylation reactions play crucial roles in controlling the activities of biomolecules. Bacterial prenyltransferases, TleC from Streptomyces blastmyceticus and MpnD from Marinactinospora thermotolerans, catalyse the 'reverse' prenylation of (-)-indolactam V at the C-7 position of the indole ring with geranyl pyrophosphate or dimethylallyl pyrophosphate, to produce lyngbyatoxin or pendolmycin, respectively. Using in vitro analyses, here we show that both TleC and MpnD exhibit relaxed substrate specificities and accept various chain lengths (C5-C25) of the prenyl donors. Comparisons of the crystal structures and their ternary complexes with (-)-indolactam V and dimethylallyl S-thiophosphate revealed the intimate structural details of the enzyme-catalysed 'reverse' prenylation reactions and identified the active-site residues governing the selection of the substrates. Furthermore, structure-based enzyme engineering successfully altered the preference for the prenyl chain length of the substrates, as well as the regio- and stereo-selectivities of the prenylation reactions, to produce a series of unnatural novel indolactams. Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases.,Mori T, Zhang L, Awakawa T, Hoshino S, Okada M, Morita H, Abe I Nat Commun. 2016 Mar 8;7:10849. doi: 10.1038/ncomms10849. PMID:26952246 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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