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Journal of Bacteriology, May 2004, p. 2872-2879, Vol. 186, No. 9
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.9.2872-2879.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Crystal Structure of the Response Regulator 02 Receiver Domain, the Essential YycF Two-Component System of Streptococcus pneumoniae in both Complexed and Native States{dagger}

Colin J. Bent,1 Neil W. Isaacs,1 Timothy J. Mitchell,2* and Alan Riboldi-Tunnicliffe2

Department of Chemistry,1 Division of Infection and Immunity, University of Glasgow, Glasgow G12 8QQ, United Kingdom2

Received 25 August 2003/ Accepted 12 January 2004

A variety of bacterial cellular responses to environmental signals are mediated by two-component signal transduction systems comprising a membrane-associated histidine protein kinase and a cytoplasmic response regulator (RR), which interpret specific stimuli and produce a measured physiological response. In RR activation, transient phosphorylation of a highly conserved aspartic acid residue drives the conformation changes needed for full activation of the protein. Sequence homology reveals that RR02 from Streptococcus pneumoniae belongs to the OmpR subfamily of RRs. The structures of the receiver domains from four members of this family, DrrB and DrrD from Thermotoga maritima, PhoB from Escherichia coli, and PhoP from Bacillus subtilis, have been elucidated. These domains are globally very similar in that they are composed of a doubly wound {alpha}5ß5; however, they differ remarkably in the fine detail of the ß4-{alpha}4 and {alpha}4 regions. The structures presented here reveal a further difference of the geometry in this region. RR02 is has been shown to be the essential RR in the gram-positive bacterium S. pneumoniae R. Lange, C. Wagner, A. de Saizieu, N. Flint, J. Molnos, M. Stieger, P. Caspers, M. Kamber, W. Keck, and K. E. Amrein, Gene 237:223-234, 1999; J. P. Throup, K. K. Koretke, A. P. Bryant, K. A. Ingraham, A. F. Chalker, Y. Ge, A. Marra, N. G. Wallis, J. R. Brown, D. J. Holmes, M. Rosenberg, and M. K. Burnham, Mol. Microbiol. 35:566-576, 2000). RR02 functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. Here we report the native structure of the receiver domain of RR02 from serotype 4 S. pneumoniae (as well as acetate- and phosphate-bound forms) at different pH levels. Two native structures at 2.3 Å, phased by single-wavelength anomalous diffraction (xenon SAD), and 1.85 Å and a third structure at pH 5.9 revealed the presence of a phosphate ion outside the active site. The fourth structure revealed the presence of an acetate molecule in the active site.

* Corresponding author. Mailing address: University of Glasgow, Division of Infection and Immunity, Joseph Black Building, University Ave., Glasgow G12 8QQ, United Kingdom. Phone: 44 141 3303749. Fax: 44 141 3303727. E-mail: t.mitchell{at}bio.gla.ac.uk.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/

Journal of Bacteriology, May 2004, p. 2872-2879, Vol. 186, No. 9
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.9.2872-2879.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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