Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS from <i>Bacillus subtilis</i>.

ABSTRACT: The bacterial flagellar motor consists of a rotor and stator units and is driven by ion flow through the stator. The activation of the ion flow is coupled with the anchoring of the stator units to the peptidoglycan layer by the stator B-subunit around the rotor. Gram-negative bacteria, such as Salmonella and Vibrio, change the conformation of the N-terminal helix of the periplasmic domain of the B-subunit to anchor the stator units. However, a recent high-speed atomic force microscopic study has suggested that the periplasmic domain of MotS, the stator B-subunit of the sodium (Na⁺)-driven stator of Bacillus subtilis, a gram-positive bacterium, unfolds at low external Na⁺ concentrations and folds at high Na⁺ concentrations to anchor the

SUBMITTER: Takekawa N 

PROVIDER: S-EPMC11853200 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature