PDBsum entry 1nxp

Signaling protein

PDB id: 1nxp

Contents

Protein chain

118 a.a. *

Ligands

PHS

Waters ×71

* Residue conservation analysis

PDB id:

1nxp

Name:

Signaling protein

Title:

Micarec ph4.5

Structure:

DNA-binding response regulator. Chain: a. Fragment: mica receiver domain. Engineered: yes

Source:

Streptococcus pneumoniae. Organism_taxid: 170187. Strain: tigr4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PDB file)

Resolution:

1.82Å R-factor: 0.184 R-free: 0.230

Authors:

C.J.Bent,N.W.Isaacs,T.J.Mitchell,A.Riboldi-Tunnicliffe

Key ref:

C.J.Bent et al. (2004). Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states. J Bacteriol, 186, 2872-2879. PubMed id: 15090529

Date:

11-Feb-03 Release date: 17-Feb-04

Protein chain

A0A0H2UQ68  (A0A0H2UQ68_STRPN) -  DNA-binding response regulator from Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

Seq: 234 a.a.

Struc: 118 a.a.

J Bacteriol 186:2872-2879 (2004)

PubMed id: 15090529

Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states.

C.J.Bent, N.W.Isaacs, T.J.Mitchell, A.Riboldi-Tunnicliffe.

ABSTRACT

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.