1vje
From Proteopedia
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Crystal structure of a autoinducer-2 synthesis protein with bound selenomethionine
Overview
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.
About this Structure
1VJE is a Single protein structure of sequence from Deinococcus radiodurans with ZN and MSE as ligands. Full crystallographic information is available from OCA.
Reference
A structural genomics approach to the study of quorum sensing: crystal structures of three LuxS orthologs., Lewis HA, Furlong EB, Laubert B, Eroshkina GA, Batiyenko Y, Adams JM, Bergseid MG, Marsh CD, Peat TS, Sanderson WE, Sauder JM, Buchanan SG, Structure. 2001 Jun;9(6):527-37. PMID:11435117
Page seeded by OCA on Wed Nov 21 04:54:21 2007
