The bacterial flagellar motor harnesses ion flow to drive rotary motion, at speeds reaching 100000 rpm and with apparently tight coupling. The functional properties of the motor are quite well understood, but its molecular mechanism remains unknown. Studies of motor physiology, together with mutational and biochemical studies of the components, place significant constraints on the mechanism. Rotation is probably driven by conformational changes in membrane-protein complexes that form the stator. These conformational changes occur as protons move on and off a critical aspartate residue in the stator protein MotB, and the resulting forces are applied to the rotor protein FliG. The bacterial flagellum is a complex structure built from about two dozen proteins. Its construction requires an apparatus at the base that exports many flagellar components to their sites of installation by way of an axial channel through the structure. The sequence of events in assembly is understood in general terms, but not yet at the molecular level. A fuller understanding of motor rotation and flagellar assembly will require more data on the structures and organization of the constituent proteins.