Long-range coupling regulates stator dynamics in the bacterial flagellar motor.

ABSTRACT: The bacterial flagellar motor is driven by stator complexes that couple ion flux to torque generation. Active stators dynamically exchange with a membrane pool in a load-dependent manner, with off-rates decreasing as motor load increases. Each stator comprises of MotA, which engages the rotor, and MotB, whose periplasmic domain anchors the complex to the peptidoglycan. But how external load regulates this anchoring remains unclear. Here, we show that long-range couplings within the Escherichia coli MotB periplasmic domain regulate stator dynamics. Computational modeling revealed that the flexible loops believed to anchor the stator to the peptidoglycan and P-ring are dynamically coupled to distant residues. Coevolutionary analysis reinforced these couplings, highlighting conserved c

SUBMITTER: Sawant SA 

PROVIDER: S-EPMC12621912 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature