Native flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries.

ABSTRACT: The bacterial flagellar MS ring is a transmembrane complex acting as the core of the flagellar motor and template for flagellar assembly. The C ring attached to the MS ring is involved in torque generation and rotation switch, and a large symmetry mismatch between these two rings has been a long puzzle, especially with respect to their role in motor function. Here, using cryoEM structural analysis of the flagellar basal body and the MS ring formed by full-length FliF from Salmonella enterica, we show that the native MS ring is formed by 34 FliF subunits with no symmetry variation. Symmetry analysis of the C ring shows a variation with a peak at 34-fold, suggesting flexibility in C ring assembly. Finally, our data also indicate that FliF subunits assume two different conformations, contribu

SUBMITTER: Kawamoto A 

PROVIDER: S-EPMC8270960 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature