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1JX6

CRYSTAL STRUCTURE OF LUXP FROM VIBRIO HARVEYI COMPLEXED WITH AUTOINDUCER-2

Summary for 1JX6
Entry DOI10.2210/pdb1jx6/pdb
DescriptorLUXP PROTEIN, CALCIUM ION, 3A-METHYL-5,6-DIHYDRO-FURO[2,3-D][1,3,2]DIOXABOROLE-2,2,6,6A-TETRAOL, ... (4 entities in total)
Functional Keywordsprotein-ligand complex, signaling protein
Biological sourceVibrio harveyi
Cellular locationPeriplasm (Probable): P54300
Total number of polymer chains1
Total formula weight39298.75
Authors
Chen, X.,Schauder, S.,Potier, N.,Van Dorsselaer, A.,Pelczer, I.,BassleR, B.L.,Hughson, F.M. (deposition date: 2001-09-05, release date: 2002-02-04, Last modification date: 2024-02-07)
Primary citationChen, X.,Schauder, S.,Potier, N.,Van Dorsselaer, A.,Pelczer, I.,Bassler, B.L.,Hughson, F.M.
Structural identification of a bacterial quorum-sensing signal containing boron.
Nature, 415:545-549, 2002
Cited by
PubMed 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.
PubMed: 11823863
DOI: 10.1038/415545a
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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