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Figure 4
Overall structure of MtHigA3 bound to DNA. (a) Superimposed cartoon representation of MtHigA3 bound to DNA and the MtHigA3 dimer structure (produced by matching the MtHigA3 dimer of both models). The MtHigA3 dimer is coloured cyan and blue. MtHigA3 bound to DNA is coloured grey. The DNA fragment of MtHigA3 bound to DNA is coloured yellow. Plot of Cα r.m.s.d. of the MtHigA3 dimer and MtHigA3 bound to DNA to compare Cα movement after DNA binding. N-terminal (Val36–His39), loop region (Ser76–His77) and C-terminal (Thr108–His113) residues show relatively large deviations. The region showing more than 1 Å r.m.s.d. is drawn in the black box and highlighted in green. (b) Cartoon and surface representation of MtHigA3 bound to the DNA structure in diverse orientations. The regions of MtHigA3 and DNA structure, which involve contact with each other, are coloured blue (MtHigA3) and yellow (DNA). Bent DNA in MtHigA3 bound to the DNA structure is marked as a red line. Promoter DNA is dramatically bent by the binding of MtHigA3 (46.5°). (c) Superimposed MtHigA3 dimer and DNA structure of MtHigA3 bound to DNA. The electrostatic surface potential of the MtHigA3 dimer is coloured between −10 kT e−1 (red) and 10 kT e−1 (blue) in two orientations rotated by 90°. The DNA structure of MtHigA3 bound to DNA is presented as a cartoon representation. DNA binds to the positively charged region of the MtHigA3 dimer.

IUCrJ
Volume 7| Part 4| July 2020| Pages 748-760
ISSN: 2052-2525
https://doi.org/10.1107/S2052252520006466