Fig. 3
Structure of the FlhAC−FliT−FliDC ternary complex. a Crystal structure of the ternary complex shown as a space-filling model. b Cartoon rendering of the structure and expanded views of the two interfaces, major and minor, between FlhAC and FliT. Residues participating in intermolecular contacts are shown as ball-and-stick. Hydrogen bonds and salt bridges are shown as broken lines. c Effect of the indicated amino acid substitutions on the affinity of FlhAC for FliT−FliDC. The effect is given as a fold decrease relative to the affinity of the wild-type proteins (Kd ~20 μM; Supplementary Fig. 4d). Non-detected binding is indicated as ND
