Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride.
The response regulator PhoP is part of the PhoQ/PhoP two-component system involved in responses to depletion of extracellular Mg(2+). Here, we report the crystal structures of the receiver domain of Escherichia coli PhoP determined in the absence and presence of the phosphoryl analog beryllofluoride. In the presence of beryllofluoride, the active receiver domain forms a twofold symmetric dimer similar to that seen in structures of other regulatory domains from the OmpR/PhoB family, providing further evidence that members of this family utilize a common mode of dimerization in the active state. In the absence of activating agents, the PhoP receiver domain crystallizes with a similar structure, consistent with the previous observation that high concentrations can promote an active state of PhoP independent of phosphorylation.
Bachhawat
Priti
P
Department of Biochemistry, Center for Advanced Biotechnology and Medicine, 679 Hoes Lane, Piscataway, NJ 08854-5627, USA.
Stock
Ann M
AM
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D001608:Beryllium / Q000494:pharmacology*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D019281:Dimerization; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D005459:Fluorides / Q000494:pharmacology*; D010766:Phosphorylation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary / Q000187:drug effects*; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; C061064:PhoP protein, Bacteria; C035982:beryllium fluoride; D001608:Beryllium; D005459:Fluorides