Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states

Priti Bachhawat, G. V.T. Swapna, Gaetano T. Montelione, Ann M. Stock

Research output: Contribution to journalArticlepeer-review

115 Scopus citations

Abstract

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 α4-β5-α5 faces, while the effector domains bind to DNA direct repeats with tandem symmetry, implying a loss of intramolecular interactions.

Original languageEnglish (US)
Pages (from-to)1353-1363
Number of pages11
JournalStructure
Volume13
Issue number9
DOIs
StatePublished - Sep 2005

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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