1UMQ

solution structure and DNA binding of the effector domain from the global regulator PrrA(RegA) from R. sphaeroides: Insights into DNA binding specificity

Summary for 1UMQ

• Entry DOI: 10.2210/pdb1umq/pdb
• NMR Information: BMRB: 5920
• Descriptor: PHOTOSYNTHETIC APPARATUS REGULATORY PROTEIN (1 entity in total)
• Functional Keywords: dna-binding protein, response regulator, dna binding domain, helix-turn-helix, sensory transduction, phosphorylation, transcription regulation, dna-binding, activator, dna binding protein
• Biological source: RHODOBACTER SPHAEROIDES
• Total number of polymer chains: 1
• Total formula weight: 9482.88

Authors

Laguri, C.,Phillips-Jones, M.K.,Williamson, M.P. (deposition date: 2003-08-28, release date: 2003-11-21, Last modification date: 2024-06-19)

Primary citation

Laguri, C.,Phillips-Jones, M.K.,Williamson, M.P.
Solution Structure and DNA Binding of the Effector Domain from the Global Regulator Prra(Rega) from Rhodobacter Sphaeroides: Insights Into DNA Binding Specificity
Nucleic Acids Res., 31:6778-, 2003

PubMed Abstract: Prr/RegA response regulator is a global transcription regulator in purple bacteria Rhodobacter sphaeroides and Rhodobacter capsulatus, and is essential in controlling the metabolic changes between aerobic and anaerobic environments. We report here the structure determination by NMR of the C-terminal effector domain of PrrA, PrrAC. It forms a three-helix bundle containing a helix-turn-helix DNA binding motif. The fold is similar to FIS protein, but the domain architecture is different from previously characterised response regulator effector domains, as it is shorter than any characterised so far. Alignment of Prr/RegA DNA targets permitted a refinement of the consensus sequence, which contains two GCGNC inverted repeats with variable half-site spacings. NMR titrations of PrrAC with specific and non-specific DNA show which surfaces are involved in DNA binding and suggest residues important for binding specificity. A model of the PrrAC/DNA complex was constructed in which two PrrAC molecules are bound to DNA in a symmetrical manner.

PubMed: 14627811
DOI: 10.1093/NAR/GKG891

Experimental method

SOLUTION NMR