Journal
JOURNAL OF BACTERIOLOGY
Volume 189, Issue 16, Pages 5987-5995Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.00049-07
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [R37 GM 047958, R37 GM047958] Funding Source: Medline
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The response regulator PhoP is part of the PhoQ/PhoP two-component system involved in responses to depletion of extracellular Mg2+. 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.
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