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Title Structure of the Polar Flagellum Reveals a Distinct Outer Membrane Complex and Its Specific Interaction with the Stator.
Journal, issue, pagesJ Bacteriol, Vol. 202, Issue 4, Year 2020
Publish dateJan 29, 2020
AuthorsShiwei Zhu / Tatsuro Nishikino / Norihiro Takekawa / Hiroyuki Terashima / Seiji Kojima / Katsumi Imada / Michio Homma / Jun Liu /
PubMed AbstractThe bacterial flagellum is a biological nanomachine that rotates to allow bacteria to swim. For flagellar rotation, torque is generated by interactions between a rotor and a stator. The stator, which ...The bacterial flagellum is a biological nanomachine that rotates to allow bacteria to swim. For flagellar rotation, torque is generated by interactions between a rotor and a stator. The stator, which is composed of MotA and MotB subunit proteins in the membrane, is thought to bind to the peptidoglycan (PG) layer, which anchors the stator around the rotor. Detailed information on the stator and its interactions with the rotor remains unclear. Here, we deployed cryo-electron tomography and genetic analysis to characterize structure of the bacterial flagellar motor in , which is best known for its polar sheathed flagellum and high-speed rotation. We determined structure of the motor at unprecedented resolution and revealed the unique protein-protein interactions among -specific features, namely the H ring and T ring. Specifically, the H ring is composed of 26 copies of FlgT and FlgO, and the T ring consists of 26 copies of a MotX-MotY heterodimer. We revealed for the first time a specific interaction between the T ring and the stator PomB subunit, providing direct evidence that the stator unit undergoes a large conformational change from a compact form to an extended form. The T ring facilitates the recruitment of the extended stator units for the high-speed motility in species. The torque of flagellar rotation is generated by interactions between a rotor and a stator; however, detailed structural information is lacking. Here, we utilized cryo-electron tomography and advanced imaging analysis to obtain a high-resolution flagellar basal body structure in , which is a Gram-negative marine bacterium. Our high-resolution motor structure not only revealed detailed protein-protein interactions among unique -specific features, the T ring and H ring, but also provided the first structural evidence that the T ring interacts directly with the periplasmic domain of the stator. Docking atomic structures of key components into the motor map allowed us to visualize the pseudoatomic architecture of the polar sheathed flagellum in spp. and provides novel insight into its assembly and function.
External linksJ Bacteriol / PubMed:31767780 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution20.0 Å
Structure data

EMDB-21027:
Vibrio flagellar motor structure
Method: EM (subtomogram averaging) / Resolution: 20.0 Å

Source
  • Vibrio alginolyticus (bacteria)

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