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http://purl.uniprot.org/citations/11435117http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11435117http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11435117http://www.w3.org/2000/01/rdf-schema#comment"

Background

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.

Results

The structure of the LuxS protein from three different bacterial species with resolutions ranging from 1.8 A to 2.4 A has been solved using an X-ray crystallographic structural genomics approach. The structure of LuxS reported here is seen to have a new alpha-beta fold. In all structures, an equivalent homodimer is observed. A metal ion identified as zinc was seen bound to a Cys-His-His triad. Methionine was found bound to the protein near the metal and at the dimer interface.

Conclusions

These structures provide support for a hypothesis that explains the in vivo action of LuxS. Specifically, acting as a homodimer, the protein binds a methionine analog, S-ribosylhomocysteine (SRH). The zinc atom is in position to cleave the ribose ring in a step along the synthesis pathway of AI-2."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.org/dc/terms/identifier"doi:10.1016/s0969-2126(01)00613-x"xsd:string
http://purl.uniprot.org/citations/11435117http://purl.org/dc/terms/identifier"doi:10.1016/s0969-2126(01)00613-x"xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Sauder J.M."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Sauder J.M."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Peat T.S."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Peat T.S."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Adams J.M."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Adams J.M."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Batiyenko Y."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Batiyenko Y."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Bergseid M.G."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Bergseid M.G."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Buchanan S.G."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Buchanan S.G."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Furlong E.B."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Furlong E.B."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Laubert B."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Laubert B."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Lewis H.A."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Lewis H.A."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Marsh C.D."xsd:string
http://purl.uniprot.org/citations/11435117http://purl.uniprot.org/core/author"Marsh C.D."xsd:string
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