Architecture of the flagellar rotor

摘要: Rotation and switching of the bacterial flagellum depends on a large rotor-mounted protein assembly composed proteins FliG, FliM FliN, with FliG most directly involved in rotation. The crystal structure complex between central domains FliM, conjunction several biochemical molecular-genetic experiments, reveals arrangement rotor. A stoichiometric mismatch (26 subunits) (34 is explained terms two distinct positions for FliM: one where it binds domain another C-terminal domain. This architecture provides structural framework addressing mechanisms motor rotation direction unifying body data performance. Recently proposed alternative models rotor assembly, based subunit contact observed crystals, are not supported by experiment.