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. 2009 Jan 7;37(4):1211–1224. doi: 10.1093/nar/gkn1046

Figure 3.

Figure 3.

Conformational plasticity of MepR. (A) Superimposition of the two subunits of the MepR dimer with subunit A colored light pink and subunit B, red. Subunits are depicted as ribbons and the location of the N- and C-termini are labelled N and C, respectively. (B) Superimposition of the MepR dimer (light pink) and DNA-bound OhrR dimer (cyan), using the entire polypeptide chain. The wHTH motifs of MepR and DNA-bound OhrR are colored red and yellow, respectively. The midpoints of the recognition helices of MepR and OhrR are shown as spheres and their intersubunit distances provided above by the arrows. (C) Superimposition of the subunits of selected MarR family members (MepR, apoOhrR, Xc OhrROxi, DNA-bound Bs OhrR, E. coli MarR, Methanobacterium MarR, and MexR). The wHTH motifs of each protein are colored light pink and labelled. The N- and C-termini of MepR are colored black and cyan, respectively, and labelled, whereas the N- and C-termini of all the other proteins are colored green and red and labelled N (green) and C (red), respectively. On the right, the overlays are rotated 180° along the y-axis.