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PDBsum entry 1nxo
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Signaling protein
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PDB id
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1nxo
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the response regulator 02 receiver domain, The essential yycf two-Component system of streptococcus pneumoniae in both complexed and native states.
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Authors
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C.J.Bent,
N.W.Isaacs,
T.J.Mitchell,
A.Riboldi-Tunnicliffe.
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Ref.
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J Bacteriol, 2004,
186,
2872-2879.
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PubMed id
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Abstract
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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(5)beta(5); however, they differ remarkably in the fine detail of the
beta4-alpha4 and alpha4 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 A, phased by single-wavelength anomalous
diffraction (xenon SAD), and 1.85 A 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.
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