1ZES

BeF3- activated PhoB receiver domain

Summary for 1ZES

• Entry DOI: 10.2210/pdb1zes/pdb
• Descriptor: Phosphate regulon transcriptional regulatory protein phoB, MAGNESIUM ION, BERYLLIUM TRIFLUORIDE ION, ... (4 entities in total)
• Functional Keywords: chey-like fold, response regulator, transcription factor, phob, activated, transcription activator
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P08402
• Total number of polymer chains: 3
• Total formula weight: 43304.42

Authors

Bachhawat, P.,Montelione, G.T.,Stock, A.M. (deposition date: 2005-04-19, release date: 2005-09-20, Last modification date: 2024-02-14)

Primary citation

Bachhawat, P.,Swapna, G.V.,Montelione, G.T.,Stock, A.M.
Mechanism of Activation for Transcription Factor PhoB Suggested by Different Modes of Dimerization in the Inactive and Active States.
Structure, 13:1353-1363, 2005

PubMed 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 alpha4-beta5-alpha5 faces, while the effector domains bind to DNA direct repeats with tandem symmetry, implying a loss of intramolecular interactions.

PubMed: 16154092
DOI: 10.1016/j.str.2005.06.006

Experimental method

X-RAY DIFFRACTION (1.9 Å)