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- W2114798043 abstract "ABSTRACT 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." @default.
- W2114798043 created "2016-06-24" @default.
- W2114798043 creator A5039365328 @default.
- W2114798043 creator A5071039030 @default.
- W2114798043 date "2007-08-15" @default.
- W2114798043 modified "2023-09-26" @default.
- W2114798043 title "Crystal Structures of the Receiver Domain of the Response Regulator PhoP from <i>Escherichia coli</i> in the Absence and Presence of the Phosphoryl Analog Beryllofluoride" @default.
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- W2114798043 doi "https://doi.org/10.1128/jb.00049-07" @default.
- W2114798043 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1952025" @default.
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