Changes in the hydrophobic network of the FliG_MC domain induce rotational switching of the flagellar motor.

ABSTRACT: The FliG protein plays a pivotal role in switching the rotational direction of the flagellar motor between clockwise and counterclockwise. Although we previously showed that mutations in the Gly-Gly linker of FliG induce a defect in switching rotational direction, the detailed molecular mechanism was not elucidated. Here, we studied the structural changes in the FliG fragment containing the middle and C-terminal regions, named FliG_MC, and the switch-defective FliG_MC-G215A, using nuclear magnetic resonance (NMR) and molecular dynamics simulations. NMR analysis revealed multiple conformations of FliG_MC, and the exchange process between these conformations was suppressed by the G215A residue substitution. Furthermore, changes in the intradomain orientation of

SUBMITTER: Nishikino T 

PROVIDER: S-EPMC10372836 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature