1VJE
Crystal structure of a autoinducer-2 synthesis protein with bound selenomethionine
Summary for 1VJE
Entry DOI | 10.2210/pdb1vje/pdb |
Descriptor | Autoinducer-2 production protein LuxS, ZINC ION, SELENOMETHIONINE, ... (4 entities in total) |
Functional Keywords | structural genomics, hydrolase |
Biological source | Deinococcus radiodurans |
Total number of polymer chains | 2 |
Total formula weight | 37368.57 |
Authors | Structural GenomiX (deposition date: 2004-02-03, release date: 2004-02-10, Last modification date: 2024-11-06) |
Primary citation | Lewis, H.A.,Furlong, E.B.,Laubert, B.,Eroshkina, G.A.,Batiyenko, Y.,Adams, J.M.,Bergseid, M.G.,Marsh, C.D.,Peat, T.S.,Sanderson, W.E.,Sauder, J.M.,Buchanan, S.G. A Structural Genomics Approach to the Study of Quorum Sensing: Crystal Structures of Three LuxS Orthologs Structure, 9:527-537, 2001 Cited by PubMed Abstract: Quorum sensing is the mechanism by which bacteria control gene expression in response to cell density. Two major quorum-sensing systems have been identified, system 1 and system 2, each with a characteristic signaling molecule (autoinducer-1, or AI-1, in the case of system 1, and AI-2 in system 2). The luxS gene is required for the AI-2 system of quorum sensing. LuxS and AI-2 have been described in both Gram-negative and Gram-positive bacterial species and have been shown to be involved in the expression of virulence genes in several pathogens. PubMed: 11435117DOI: 10.1016/S0969-2126(01)00613-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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