Journal
STRUCTURE
Volume 13, Issue 9, Pages 1353-1363Publisher
CELL PRESS
DOI: 10.1016/j.str.2005.06.006
Keywords
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [R37GM047958, R37 GM047958, P50 GM062413] Funding Source: Medline
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Response regulators (RRs), which undergo phosphorylation/dephosphorylation at aspartate residues, are highly prevalent in bacterial signal transduction. RRs typically contain an N-terminal receiver domain that regulates the activities of a C-terminal DNA binding domain in a phosphorylation-dependent manner. We present crystallography and solution NMR data for the receiver domain of Escherichia coli PhoB which show distinct 2-fold symmetric dimers in the inactive and active states. These structures, together with the previously determined structure of the C-terminal domain of PhoB bound to DNA, define the conformation of the active transcription factor and provide a model for the mechanism of activation in the OmpR/PhoB subfamily, the largest group of RRs. In the active state, the receiver domains dimerize with 2-fold rotational symmetry using their alpha 4-beta 5-alpha 5 faces, while the effector domains bind to DNA direct repeats with tandem symmetry, implying a loss of intramolecular interactions.
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