Deciphering the Conformational Change of Bacterial Flagellar Rotor Protein FliG, That Determines the Rotational Direction of the Flagellar Motor, by High-Pressure Solution NMR Analysis

Abstract

The nuclear magnetic resonance (NMR) measurements under high pressure conditions are powerful technique for characterizing protein properties and its conformational changes. Bacterial flagellum is a molecular nano-machine and bacteria move toward favorable condition for survive and growth to rotate flagellar motor, although the molecular mechanism of the motor rotation is still unclear. In this article, we introduce our recently published results that clarified the determination mechanism of the rotational direction by analyzing of FliG, a flagellar rotor protein. Combining the structural analysis of solution NMR and the measurement of high-pressure condition, we revealed that the rearrangement of interaction network in FliG determines the rotational direction.