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5N6H

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

5N6H の概要
エントリーDOI10.2210/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: 28675161
DOI: 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)
構造検証レポート
Validation report summary of 5n6h
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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