Structural identification of a bacterial quorum-sensing signal containing boron. Author Xin Chen, Stephan Schauder, Noelle Potier, Alain Van Dorsselaer, István Pelczer, Bonnie Bassler, Frederick Hughson Publication Year 2002 Type Journal Article Abstract 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. Keywords Vibrio, Escherichia coli, Bacterial Proteins, Signal Transduction, Lactones, Models, Molecular, Crystallography, X-Ray, Recombinant Fusion Proteins, Homoserine, Boron, Borates, Bridged Bicyclo Compounds, Heterocyclic Journal Nature Volume 415 Issue 6871 Pages 545-9 Date Published 2002 Jan 31 ISSN Number 0028-0836 DOI 10.1038/415545a Alternate Journal Nature PMID 11823863 PubMedGoogle ScholarBibTeXEndNote X3 XML