+検索条件
-Structure paper
タイトル | The tetrameric MotA complex as the core of the flagellar motor stator from hyperthermophilic bacterium. |
---|---|
ジャーナル・号・ページ | Sci Rep, Vol. 6, Page 31526, Year 2016 |
掲載日 | 2016年8月17日 |
著者 | Norihiro Takekawa / Naoya Terahara / Takayuki Kato / Mizuki Gohara / Kouta Mayanagi / Atsushi Hijikata / Yasuhiro Onoue / Seiji Kojima / Tsuyoshi Shirai / Keiichi Namba / Michio Homma / |
PubMed 要旨 | Rotation of bacterial flagellar motor is driven by the interaction between the stator and rotor, and the driving energy is supplied by ion influx through the stator channel. The stator is composed of ...Rotation of bacterial flagellar motor is driven by the interaction between the stator and rotor, and the driving energy is supplied by ion influx through the stator channel. The stator is composed of the MotA and MotB proteins, which form a hetero-hexameric complex with a stoichiometry of four MotA and two MotB molecules. MotA and MotB are four- and single-transmembrane proteins, respectively. To generate torque, the MotA/MotB stator unit changes its conformation in response to the ion influx, and interacts with the rotor protein FliG. Here, we overproduced and purified MotA of the hyperthermophilic bacterium Aquifex aeolicus. A chemical crosslinking experiment revealed that MotA formed a multimeric complex, most likely a tetramer. The three-dimensional structure of the purified MotA, reconstructed by electron microscopy single particle imaging, consisted of a slightly elongated globular domain and a pair of arch-like domains with spiky projections, likely to correspond to the transmembrane and cytoplasmic domains, respectively. We show that MotA molecules can form a stable tetrameric complex without MotB, and for the first time, demonstrate the cytoplasmic structure of the stator. |
リンク | Sci Rep / PubMed:27531865 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 25.0 Å |
構造データ | EMDB-3417: |
由来 |
|