9LJK

Structure of the periplasmic domain of MotS from Bacillus subtilis

9LJK の概要

• エントリーDOI: 10.2210/pdb9ljk/pdb
• 分子名称: Flagellar motor protein MotS, SULFATE ION (3 entities in total)
• 機能のキーワード: bacterial flagellum, stator protein, peptidoglycan binding, motor protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41901.40

構造登録者

Nishiuchi, K.,Takekawa, N.,Imada, K. (登録日: 2025-01-15, 公開日: 2025-02-26, 最終更新日: 2025-03-19)

主引用文献

Takekawa, N.,Yamaguchi, A.,Nishiuchi, K.,Uehori, M.,Kinoshita, M.,Minamino, T.,Imada, K.
Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS from Bacillus subtilis.
Biomolecules, 15:-, 2025

PubMed 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 and , 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 , a gram-positive bacterium, unfolds at low external Na concentrations and folds at high Na concentrations to anchor the stator units. Here, we report the crystal structures of MotS, a periplasmic fragment of MotS, from at high and low Na concentrations. We also performed far-UV CD spectroscopic analysis of the wild-type MotS and MotS proteins and mutant variants of MotS under high and low Na concentrations and found that the N-terminal disordered region of MotS shows a Na-dependent coil-helix transition. We propose a mechanism of the Na-dependent structural transition of Bs-MotS to anchor the stator units.

PubMed: 40001605
DOI: 10.3390/biom15020302

実験手法

X-RAY DIFFRACTION (1.89 Å)