5n6l

Structure of the membrane integral lipoprotein N-acyltransferase Lnt C387A mutant from E. coli

spinqualitylabelsall models 5n6l, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n6l is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, OLC Gene: lnt, cutE, b0657, JW0654 (ECOLI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LNT_ECOLI] Transfers the fatty acyl group on membrane lipoproteins. Publication Abstract from PubMed Lipoproteins serve essential roles in the bacterial cell envelope. The posttranslational modification pathway leading to lipoprotein synthesis involves three enzymes. All are potential targets for the development of new antibiotics. Here we report the crystal structure of the last enzyme in the pathway, apolipoprotein N-acyltransferase, Lnt, responsible for adding a third acyl chain to the lipoprotein's invariant diacylated N-terminal cysteine. Structures of Lnt from Pseudomonas aeruginosa and Escherichia coli have been solved; they are remarkably similar. Both consist of a membrane domain on which sits a globular periplasmic domain. The active site resides above the membrane interface where the domains meet facing into the periplasm. The structures are consistent with the proposed ping-pong reaction mechanism and suggest plausible routes by which substrates and products enter and leave the active site. While Lnt may present challenges for antibiotic development, the structures described should facilitate design of therapeutics with reduced off-target effects. Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis.,Wiktor M, Weichert D, Howe N, Huang CY, Olieric V, Boland C, Bailey J, Vogeley L, Stansfeld PJ, Buddelmeijer N, Wang M, Caffrey M Nat Commun. 2017 Jul 4;8:15952. doi: 10.1038/ncomms15952. PMID:28675161 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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