2HJE

Crystal structure of Vibrio harveyi LuxQ periplasmic domain

Summary for 2HJE

• Entry DOI: 10.2210/pdb2hje/pdb
• Related: 2hj9
• Descriptor: Autoinducer 2 sensor kinase/phosphatase luxQ, NICKEL (II) ION (3 entities in total)
• Functional Keywords: per/arnt/simple-minded (pas) fold, autoinducer-2 (ai-2), quorum sensing, histidine sensor kinase, signaling protein
• Biological source: Vibrio harveyi
• Cellular location: Cell inner membrane; Multi-pass membrane protein (Probable): P54302
• Total number of polymer chains: 1
• Total formula weight: 25103.64

Authors

Neiditch, M.B.,Kelly, R.C.,Hughson, F.M. (deposition date: 2006-06-30, release date: 2006-09-26, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)