Modeling bacterial flagellar motor with new structure information: Rotational dynamics of two interacting protein nano-rings

TL;DR

This paper presents a new mathematical model of the bacterial flagellar motor based on recent structural discoveries, predicting dynamics of interacting protein rings and aligning with observed torque-speed behavior.

Contribution

It introduces a structure-informed model of the bacterial flagellar motor featuring two rotating protein rings, offering new insights into its molecular torque generation mechanism.

Findings

Model predicts load-dependent rotor and stator dynamics.

Results align with observed torque-speed relation.

Model suggests testable predictions for future experiments.

Abstract

In this article, we develop a mathematical model for the rotary bacterial flagellar motor (BFM) based on the recently discovered structure of the stator complex (MotA$_5$MotB$_2$). The structure suggested that the stator also rotates. The BFM is modeled as two rotating nano-rings that interact with each other. Specifically, translocation of protons through the stator complex drives rotation of the MotA pentamer ring, which in turn drives rotation of the FliG ring in the rotor via interactions between the MotA ring of the stator and the FliG ring of the rotor. Preliminary results from the structure-informed model are consistent with the observed torque-speed relation. More importantly, the model predicts distinctive rotor and stator dynamics and their load dependence, which may be tested by future experiments. Possible approaches to verify and improve the model to further understanding of the molecular mechanism for torque generation in BFM are also discussed.