2HJE

Crystal structure of Vibrio harveyi LuxQ periplasmic domain

2HJE の概要

• エントリーDOI: 10.2210/pdb2hje/pdb
• 関連するPDBエントリー: 2hj9
• 分子名称: Autoinducer 2 sensor kinase/phosphatase luxQ, NICKEL (II) ION (3 entities in total)
• 機能のキーワード: per/arnt/simple-minded (pas) fold, autoinducer-2 (ai-2), quorum sensing, histidine sensor kinase, signaling protein
• 由来する生物種: Vibrio harveyi
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein (Probable): P54302
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25103.64

構造登録者

Neiditch, M.B.,Kelly, R.C.,Hughson, F.M. (登録日: 2006-06-30, 公開日: 2006-09-26, 最終更新日: 2024-02-14)

主引用文献

Neiditch, M.B.,Federle, M.J.,Pompeani, A.J.,Kelly, R.C.,Swem, D.L.,Jeffrey, P.D.,Bassler, B.L.,Hughson, F.M.
Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.
Cell(Cambridge,Mass.), 126:1095-1108, 2006

PubMed Abstract: Bacteria sense their environment using receptors of the histidine sensor kinase family, but how kinase activity is regulated by ligand binding is not well understood. Autoinducer-2 (AI-2), a secreted signaling molecule originally identified in studies of the marine bacterium Vibrio harveyi, regulates quorum-sensing responses and allows communication between different bacterial species. AI-2 signal transduction in V. harveyi requires the integral membrane receptor LuxPQ, comprised of periplasmic binding protein (LuxP) and histidine sensor kinase (LuxQ) subunits. Combined X-ray crystallographic and functional studies show that AI-2 binding causes a major conformational change within LuxP, which in turn stabilizes a quaternary arrangement in which two LuxPQ monomers are asymmetrically associated. We propose that formation of this asymmetric quaternary structure is responsible for repressing the kinase activity of both LuxQ subunits and triggering the transition of V. harveyi into quorum-sensing mode.

PubMed: 16990134
DOI: 10.1016/j.cell.2006.07.032

実験手法

X-RAY DIFFRACTION (1.7 Å)