Extended Data Fig. 7: CheY3-P binding triggers conformational change.
From: Molecular mechanism for rotational switching of the bacterial flagellar motor
a-d, Comparison between the C-ring models before (grey, top left in each panel) and after (colored, top right in each panel) CheY3-P binding. e, The dash framed regions in panel a are overlapped to show their differences. The N-terminal domain of FliM (FliMN) folds out ~154Ëš to interact with CheY3-P. f, Binding of CheY3-P induces ~27Ëš tilt of the FliM middle domain (FliMM). g, h, FliG2 undergoes a large tilt and alters the interactions between FliG2 and MotA. The charged residues (Lys275, Arg292, Glu299, and Asp300) in the C-terminal domain of FliG2 (FliG2C) are colored in red.
