期刊
PROTEIN SCIENCE
卷 14, 期 12, 页码 3077-3088出版社
WILEY
DOI: 10.1110/ps.051722805
关键词
phosphorylation; transcription regulation; response regulator; TMAO respiratory system; Kdp K+ transport system
资金
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [R37GM047958, T32GM08319, T32 GM008319, F31 GM070142, 5F31GM070142, R37 GM047958] Funding Source: Medline
Bacterial response regulators are key regulatory proteins that function as the final elements of so-called two-component signaling systems. The activities of response regulators in vivo are modulated by phosphorylation that results from interactions between the response regulator and its cognate histidine protein kinase. The level of response regulator phosphorylation, which is regulated by intra-or extracellular signals sensed by the histidine protein kinase, ultimately determines the output response that is initiated or carried out by the response regulator. We have recently hypothesized that in the OmpR/PhoB subfamily of response regulator transcription factors, this activation involves a common mechanism of dimerization using a set of highly conserved residues in the alpha 4-beta 5-alpha 5 face. Here we report the X-ray crystal structures of the regulatory domains of response regulators TorR (1.8 angstrom), Ca2+-bound KdpE (2.0 angstrom), and Mg2+/BeF3--bound KdpE (2.2 angstrom), both members of the OmpR/ PhoB subfamily from Escherichia coli. Both regulatory domains form symmetric dimers in the asymmetric unit that involve the alpha 4-beta 5-alpha 5 face. As observed previously in other OmpR/PhoB response regulators, the dimer interfaces are mediated by highly conserved residues within this subfamily. These results provide further evidence that most all response regulators of the OmpR/ PhoB subfamily share a common mechanism of activation by dimerization.
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