2HJ9
Crystal structure of the Autoinducer-2-bound form of Vibrio harveyi LuxP complexed with the periplasmic domain of LuxQ
Summary for 2HJ9
| Entry DOI | 10.2210/pdb2hj9/pdb |
| Related | 1JX6 1ZHH 2hje |
| Descriptor | Autoinducer 2-binding periplasmic protein luxP, Autoinducer 2 sensor kinase/phosphatase luxQ, 3A-METHYL-5,6-DIHYDRO-FURO[2,3-D][1,3,2]DIOXABOROLE-2,2,6,6A-TETRAOL, ... (4 entities in total) |
| Functional Keywords | periplasmic binding protein, per/arnt/simple-minded (pas) fold, autoinducer-2 (ai-2), quorum sensing, histidine sensor kinase, signaling protein |
| Biological source | Vibrio harveyi More |
| Cellular location | Periplasm (Probable): P54300 Cell inner membrane; Multi-pass membrane protein (Probable): P54302 |
| Total number of polymer chains | 4 |
| Total formula weight | 127602.31 |
| Authors | Neiditch, M.B.,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 Cited by 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: 16990134DOI: 10.1016/j.cell.2006.07.032 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.34 Å) |
Structure validation
Download full validation report
