CryoEM structures reveal how the bacterial flagellum rotates and switches direction

Bacterial chemotaxis requires bidirectional flagellar rotation at different rates. Rotation is driven by a flagellar motor, which is a supercomplex containing multiple rings. Architectural uncertainty regarding the cytoplasmic C-ring, or 'switch', limits our understanding of how the motor transmits torque and direction to the flagellar rod. Here we report cryogenic electron microscopy structures for Salmonella enterica serovar typhimurium inner membrane MS-ring and C-ring in a counterclockwise pose (4.0 angstrom) and isolated C-ring in a clockwise pose alone (4.6 angstrom) and bound to a regulator (5.9 angstrom). Conformational differences between rotational poses include a 180 degrees shift in FliF/FliG domains that rotates the outward-facing MotA/B binding site to inward facing. The regulator has specificity for the clockwise pose by bridging elements unique to this conformation. We used these structures to propose how the switch reverses rotation and transmits torque to the flagellum, which advances the understanding of bacterial chemotaxis and bidirectional motor rotation. CryoEM of the Salmonella MS- and C-rings in a counterclockwise pose and the C-ring in clockwise poses reveal structural insight into the mechanisms of directional switches and torque transmission for the bacterial flagellar supercomplex.