1JVI

THE 2.2 ANGSTROM RESOLUTION STRUCTURE OF BACILLUS SUBTILIS LUXS/RIBOSILHOMOCYSTEINE COMPLEX

1JVI の概要

• エントリーDOI: 10.2210/pdb1jvi/pdb
• 関連するPDBエントリー: 1J98 1JQW
• 分子名称: Autoinducer-2 production protein luxS, ZINC ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: autoinducer synthesis, signaling protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18354.17

構造登録者

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. (登録日: 2001-08-30, 公開日: 2001-10-24, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)