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

与质子驱动的鞭毛马达相比，人们认为即使在钠驱动的鞭毛马达中，转子组件FliG的C-端区也具有产生旋转力的重要残基，然而，在钠驱动的马达中，保守的带电残基并不给出关键的结果。目前尚不清楚直接参与转子和定子之间相互作用的关键残基是什么。在本研究中，利用核磁共振技术确定了FliG的C-末端95%的结构，以直观地显示FliG与转子的相互作用，并对FliG的重要相互作用残基进行了归属。

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.