1jx6 | pdb_00001jx6
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CRYSTAL STRUCTURE OF LUXP FROM VIBRIO HARVEYI COMPLEXED WITH AUTOINDUCER-2
Overview
Cell-cell communication in bacteria is accomplished through the exchange, of extracellular signalling molecules called autoinducers. This process, termed quorum sensing, allows bacterial populations to coordinate gene, expression. Community cooperation probably enhances the effectiveness of, processes such as bioluminescence, virulence factor expression, antibiotic, production and biofilm development. Unlike other autoinducers, which are, specific to a particular species of bacteria, a recently discovered, autoinducer (AI-2) is produced by a large number of bacterial species., AI-2 has been proposed to serve as a 'universal' signal for inter-species, communication. The chemical identity of AI-2 has, however, proved elusive., Here we present the crystal structure of an AI-2 sensor protein, LuxP, in, a complex with autoinducer. The bound ligand is a furanosyl borate diester, that bears no resemblance to previously characterized autoinducers. Our, findings suggest that addition of naturally occurring borate to an AI-2, precursor generates active AI-2. Furthermore, they indicate a potential, biological role for boron, an element required by a number of organisms, but for unknown reasons.
About this Structure
1JX6 is a Single protein structure of sequence from Vibrio harveyi with CA and AI2 as ligands. Full crystallographic information is available from OCA.
Reference
Structural identification of a bacterial quorum-sensing signal containing boron., Chen X, Schauder S, Potier N, Van Dorsselaer A, Pelczer I, Bassler BL, Hughson FM, Nature. 2002 Jan 31;415(6871):545-9. PMID:11823863
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