Fig. 4
Structure of the FlhAC−FliS−FliCC ternary complex. a Crystal structure of the ternary complex shown as a space-filling model. b Cartoon rendering of the structure and expanded view of the interacting regions between FlhAC and FliT. Residues participating in intermolecular contacts are shown as ball-and-stick. Hydrogen bond is shown as broken lines. c Effect of the indicated amino acid substitutions on the affinity of FlhAC for FliS−FliCC. The effect is given as a fold decrease relative to the affinity of the wild-type proteins (Kd ~10 μM; Supplementary Fig. 5d). Non-detected binding is indicated as ND
