Tuning the stator subunit of the flagellar motor with coiled-coil engineering.

ABSTRACT: Many bacteria swim driven by an extracellular filament rotated by the bacterial flagellar motor. This motor is powered by the stator complex, MotA₅ MotB₂ , an heptameric complex which forms an ion channel which couples energy from the ion motive force to torque generation. Recent structural work revealed that stator complex consists of a ring of five MotA subunits which rotate around a central dimer of MotB subunits. Transmembrane (TM) domains TM3 and TM4 from MotA combine with the single TM domain from MotB to form two separate ion channels within this complex. Much is known about the ion binding site and ion specificity; however, to date, no modeling has been undertaken to explore the MotB-MotB dimer stability and the role of MotB conformational dynamics during rota

SUBMITTER: Ridone P 

PROVIDER: S-EPMC10659934 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature