Fig. 5: CymA interferes with Mtb ClpC2 binding to its promoter DNA.

a Surface representation of ClpC294–252-CymA coloured according to residue conservation produced using ConSurf60,61,62. CymA is coloured in orange and shown in stick representation. b Structure of ClpC294–252 depicting surface charge and shown in the same orientation as in a. c Close-up of the suggested DNA recognition helix shown in the forefront. Arginines suggested to contribute to DNA-binding are shown in stick representation. d Comparison of ClpC2 WT and ClpC2 R185A/R189A double mutant in an electrophoretic mobility shift assay. ClpC2 variants were titrated against 0.5 nM DNA probe and loaded onto a 12% polyacrylamide gel. Data are representative of three independent experiments.