Analysis of the structural dynamics of the flagellar motor proteins using NMR

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Compared with the proton-driven flagellar motor, it is believed that even in the sodium-driven flagellar motor, the C-terminal region of a rotor component FliG has important residues to produce the rotational force, however, the conserved charged residues did not give a critical result in sodium-driven motor. It has not been clarified to identify the key residues involved in the interaction directly between the residues of rotor and stator. In this study, the structure of C-terminal region of FliG was determined at 95% using NMR to show the interaction with the rotor directly and to assign the important interaction residues of FliG.