5N6H
Structure of the membrane integral lipoprotein N-acyltransferase Lnt from E. coli
5N6H の概要
| エントリーDOI | 10.2210/pdb5n6h/pdb |
| 分子名称 | Apolipoprotein N-acyltransferase, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | membrane protein, lipoprotein, n-acyltransferase, lipidic cubic phase |
| 由来する生物種 | Escherichia coli (strain K12) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 126176.47 |
| 構造登録者 | Huang, C.-Y.,Boland, C.,Howe, N.,Wiktor, M.,Vogeley, L.,Weichert, D.,Bailey, J.,Olieric, V.,Wang, M.,Caffrey, M. (登録日: 2017-02-15, 公開日: 2017-07-12, 最終更新日: 2024-05-08) |
| 主引用文献 | Wiktor, M.,Weichert, D.,Howe, N.,Huang, C.Y.,Olieric, V.,Boland, C.,Bailey, J.,Vogeley, L.,Stansfeld, P.J.,Buddelmeijer, N.,Wang, M.,Caffrey, M. Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis. Nat Commun, 8:15952-15952, 2017 Cited by PubMed Abstract: 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. PubMed: 28675161DOI: 10.1038/ncomms15952 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.9 Å) |
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