Summary information and primary citation

5w43; DSSR-derived features in text and JSON formats
DNA binding protein
X-ray (3.15 Å)
Structure of the two-component response regulator rcsb-DNA complex
Filippova EV, Zemaitaitis B, Aung T, Wolfe AJ, Anderson WF (2018): "Structural Basis for DNA Recognition by the Two-Component Response Regulator RcsB." MBio, 9. doi: 10.1128/mBio.01993-17.
RcsB is a highly conserved transcription regulator of the Rcs phosphorelay system, a complex two-component signal transduction system (N. Majdalani and S. Gottesman, Annu Rev Microbiol 59:379-405, 2005; A. J. Wolfe, Curr Opin Microbiol 13:204-209, 2010,; D. J. Clarke, Future Microbiol 5:1173-1184, 2010, RcsB plays an important role in virulence and pathogenicity in human hosts by regulating biofilm formation. RcsB can regulate transcription alone or together with its auxiliary transcription regulators by forming heterodimers. This complexity allows RcsB to regulate transcription of more than 600 bacterial genes in response to different stresses (D. Wang et al., Mol Plant Microbe Interact 25:6-17, 2012, Despite increasing knowledge of RcsB importance, molecular mechanisms that drive the ability of RcsB to control transcription of a large number of genes remain unclear. Here, we present crystal structures of unphosphorylated RcsB in complex with the consensus DNA-binding sequence of 22-mer (DNA22) and 18-mer (DNA18) of theflhDCoperon fromEscherichia colidetermined at 3.15- and 3.37-Å resolution, respectively. The results of our structural analysis combined with the results ofin vitrobinding assays provide valuable insights to the protein regulatory mechanism, demonstrate how RcsB recognizes target DNA sequences, and reveal a unique oligomeric state that allows RcsB to form homo- and heterodimers. This information will help us understand the complex mechanisms of transcriptional regulation by RcsB in bacteria.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js