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1ZHH

Crystal Structure of the Apo Form of Vibrio Harveyi LUXP Complexed with the Periplasmic Domain of LUXQ

1ZHH の概要
エントリーDOI10.2210/pdb1zhh/pdb
分子名称Autoinducer 2-binding periplasmic protein luxP, Autoinducer 2 sensor kinase/phosphatase luxQ, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, ... (4 entities in total)
機能のキーワードperiplasmic binding protein, per/arnt/simple-minded (pas) fold, autoinducer-2 (ai-2), quorum sensing, sensor kinase, signaling protein
由来する生物種Vibrio harveyi
詳細
細胞内の位置Periplasm (Probable): P54300
Cell inner membrane; Multi-pass membrane protein (Probable): P54302
タンパク質・核酸の鎖数2
化学式量合計66909.97
構造登録者
Neiditch, M.B.,Federle, M.J.,Miller, S.T.,Bassler, B.L.,Hughson, F.M. (登録日: 2005-04-25, 公開日: 2005-05-24, 最終更新日: 2024-02-14)
主引用文献Neiditch, M.B.,Federle, M.J.,Miller, S.T.,Bassler, B.L.,Hughson, F.M.
Regulation of LuxPQ Receptor Activity by the Quorum-Sensing Signal Autoinducer-2.
Mol.Cell, 18:507-518, 2005
Cited by
PubMed Abstract: The extracellular signaling molecule autoinducer-2 (AI-2) mediates quorum-sensing communication in diverse bacterial species. In marine vibrios, binding of AI-2 to the periplasmic receptor LuxP modulates the activity of the inner membrane sensor kinase LuxQ, transducing the AI-2 information into the cytoplasm. Here, we show that Vibrio harveyi LuxP associates with LuxQ in both the presence and absence of AI-2. The 1.9 A X-ray crystal structure of apoLuxP, complexed with the periplasmic domain of LuxQ, reveals that the latter contains two tandem Per/ARNT/Simple-minded (PAS) folds. Thus, although many prokaryotic PAS folds themselves bind ligands, the LuxQ periplasmic PAS folds instead bind LuxP, monitoring its AI-2 occupancy. Mutations that disrupt the apoLuxP:LuxQ interface sensitize V. harveyi to AI-2, implying that AI-2 binding causes the replacement of one set of LuxP:LuxQ contacts with another. These conformational changes switch LuxQ between two opposing enzymatic activities, each of which conveys information to the cytoplasm about the cell density of the surrounding environment.
PubMed: 15916958
DOI: 10.1016/j.molcel.2005.04.020
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.94 Å)
構造検証レポート
Validation report summary of 1zhh
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2026-04-29に公開中

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