1umq

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

spinqualitylabelsall models 1umq Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1umq is a 1 chain structure with sequence from Cereibacter sphaeroides. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function REGA_CERS4 Member of the two-component regulatory system RegB/RegA. Involved in transactivating anaerobic expression of the photosynthetic apparatus. It is a transcriptional regulator that is responsible for activating expression of the puf, puh, and puc operons in response to a decrease in oxygen tension. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificity.,Laguri C, Phillips-Jones MK, Williamson MP Nucleic Acids Res. 2003 Dec 1;31(23):6778-87. PMID:14627811 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Response regulator 3D structure

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