The flagellar stator unit is an oligomeric complex of two membrane proteins (MotA 5 B 2 ) that powers bi-directional rotation of the bacterial flagellum. Harnessing the ion motive force across the cytoplasmic membrane, the stator unit operates as a miniature rotary motor itself to provide torque for rotation of the flagellum. Recent cryo-electron microscopic (cryo-EM) structures of the stator unit provided novel insights into its assembly, function, and subunit stoichiometry, revealing the ion flux pathway and the torque generation mechanism. Furthermore, in situ cryoelectron tomography (cryo-ET) studies revealed unprecedented details of the interactions between stator unit and rotor. In this review, we summarize recent advances in our understanding of the structure and function of the flagellar stator unit, torque generation, and directional switching of the motor.
The bacterial flagellum and its rotary motorMany bacteria, including Escherichia coli, Salmonella, and Bacillus spp., use flagella (see Glossary) to move through liquid environments and across surfaces. The flagellum is a supramolecular nanomachine that protrudes from the cell envelope and measures~5-20 μm in length. It is able to rotate in both clockwise (CW) and counterclockwise (CCW) directions to propel the bacterial cell body in different living environments [1,2]. Rotational switching between these two modes is regulated by chemotactic signaling, which is a rapid process that responds to environmental stimuli and biases movement of the cell toward attractants and away from repellents. Flagella-mediated chemotaxis further enables pathogenic bacteria to move toward cells to establish in vivo niches. [3,4]. Thus, flagella have fundamental roles in bacterial locomotion and virulence [5].The flagellum comprises more than 25 kinds of building blocks, which assemble in a highly ordered manner. The flagellar structure can be divided into three morphologically distinguishable parts: a cell envelope-spanning motor (basal body), a universal joint (hook), and a long, thin helical filament [6,7] (Figure 1). Among them, the most intricate part is the basal body, containing the components responsible for assembly of the flagellum [the flagellar-specific type-III secretion system (T3SS) [8]], torque generation (the stator units [9]), and rotational switching (binding of the response regulator CheY-P to the cytoplasmic C-ring [10,11]). Cryo-ET studies of the motor from different bacterial species show the variation of its structure, while the core components are conserved [7,12,13]. For example, in the Gram-negative bacteria Salmonella and E. coli, the flagellar motor contains four ring-like structures based on their distributions relative to the cell surface layers [lipopolysaccharide (L-)ring, peptidoglycan (P-)ring, inner membrane/ supramembrane (MS-)ring, and cytoplasmic (C-)ring] surrounding a central rigid rod [14][15][16][17]. Additional ring-like structures, H-and T-rings, located in the periplasmic space, have also been observed in Vibrio spp [18]. It i...