1JQW

THE 2.3 ANGSTROM RESOLUTION STRUCTURE OF BACILLUS SUBTILIS LUXS/HOMOCYSTEINE COMPLEX

Summary for 1JQW

• Entry DOI: 10.2210/pdb1jqw/pdb
• Related: 1J98
• Descriptor: Autoinducer-2 production protein luxS, ZINC ION, 2-AMINO-4-MERCAPTO-BUTYRIC ACID, ... (4 entities in total)
• Functional Keywords: autoinducer synthesis, signaling protein
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 18261.18

Authors

Ruzheinikov, S.N.,Das, S.K.,Sedelnikova, S.E.,Hartley, A.,Foster, S.J.,Horsburgh, M.J.,Cox, A.G.,McCleod, C.W.,Mekhalfia, A.,Blackburn, G.M.,Rice, D.W.,Baker, P.J. (deposition date: 2001-08-09, release date: 2001-10-24, Last modification date: 2024-04-03)

Primary citation

Ruzheinikov, S.N.,Das, S.K.,Sedelnikova, S.E.,Hartley, A.,Foster, S.J.,Horsburgh, M.J.,Cox, A.G.,McCleod, C.W.,Mekhalfia, A.,Blackburn, G.M.,Rice, D.W.,Baker, P.J.
The 1.2 A structure of a novel quorum-sensing protein, Bacillus subtilis LuxS
J.Mol.Biol., 313:111-122, 2001

PubMed Abstract: In bacteria, the regulation of gene expression in response to changes in cell density is called quorum sensing. The autoinducer-2 production protein LuxS, is involved in a novel quorum-sensing system and is thought to catalyse the degradation of S-ribosylhomocysteine to homocysteine and the autoinducer molecule 4,5-dihydroxy-2,3-pentadione. The crystal structure of Bacillus subtilis LuxS has been determined at 1.2 A resolution, together with the binary complexes of LuxS with S-ribosylhomocysteine and homocysteine to 2.2 and 2.3 A resolution, respectively. These structures show that LuxS is a homodimer with an apparently novel fold based on an eight-stranded beta-barrel, flanked by six alpha-helices. Each active site contains a zinc ion coordinated by the conserved residues His54, His58 and Cys126, and includes residues from both subunits. S-ribosylhomocysteine binds in a deep pocket with the ribose moiety adjacent to the enzyme-bound zinc ion. Access to the active site appears to be restricted and possibly requires conformational changes in the protein involving the movement of residues 125-129 and those at the N terminus. The structure contains an oxidised cysteine residue in the active site whose role in the biological process of LuxS has not been determined. The autoinducer-2 signalling pathway has been linked to aspects of bacterial virulence and pathogenicity. The structural data on LuxS will provide opportunities for targeting this enzyme for the rational design of new antibiotics.

PubMed: 11601850
DOI: 10.1006/jmbi.2001.5027

Experimental method

X-RAY DIFFRACTION (2.3 Å)