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Figure 1
Overall structure of Rot and its DNA-binding properties. (a) Fluorescence polarization assay of the interaction of Rot with dsDNA oligonucleotides of different lengths. (b) Two views of the Rot dimer. Monomer A is shown as a cartoon coloured magenta and monomer B is coloured cyan. (c) Sequence alignment of Rot, SarA, SarT, SarV and SarR. The secondary-structural elements of Rot are shown at the top of the sequence. α-Helices are coloured red and β-strands are coloured yellow. The conserved hydrophobic residues involved in building up the large hydrophobic environment to sustain the winged-helix motif are highlighted in black. The residues involved in binding to DNA are highlighted in blue. The sequence extension (residues 120–133) at the tail of Rot is marked by a green box. |