3HJL

The structure of full-length FliG from Aquifex aeolicus

3HJL の概要

• エントリーDOI: 10.2210/pdb3hjl/pdb
• 分子名称: Flagellar motor switch protein fliG (2 entities in total)
• 機能のキーワード: armadillo repeat motif, superhelix, conformational plasticity, fold repeat, torque generation, bacterial flagellar motor, chemotaxis, rotary motor, switch complex, biological energy conversion, bacterial flagellum, cell inner membrane, cell membrane, flagellar rotation, membrane, proton transport
• 由来する生物種: Aquifex aeolicus
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): O66891
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37141.33

構造登録者

Lee, L.K.,Ginsburg, M.A.,Crovace, C.,Donohoe, M.,Stock, D. (登録日: 2009-05-22, 公開日: 2010-08-04, 最終更新日: 2024-03-20)

主引用文献

Lee, L.K.,Ginsburg, M.A.,Crovace, C.,Donohoe, M.,Stock, D.
Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching
Nature, 466:996-1000, 2010

PubMed Abstract: The flagellar motor drives the rotation of flagellar filaments at hundreds of revolutions per second, efficiently propelling bacteria through viscous media. The motor uses the potential energy from an electrochemical gradient of cations across the cytoplasmic membrane to generate torque. A rapid switch from anticlockwise to clockwise rotation determines whether a bacterium runs smoothly forward or tumbles to change its trajectory. A protein called FliG forms a ring in the rotor of the flagellar motor that is involved in the generation of torque through an interaction with the cation-channel-forming stator subunit MotA. FliG has been suggested to adopt distinct conformations that induce switching but these structural changes and the molecular mechanism of switching are unknown. Here we report the molecular structure of the full-length FliG protein, identify conformational changes that are involved in rotational switching and uncover the structural basis for the formation of the FliG torque ring. This allows us to propose a model of the complete ring and switching mechanism in which conformational changes in FliG reverse the electrostatic charges involved in torque generation.

PubMed: 20676082
DOI: 10.1038/nature09300

実験手法

X-RAY DIFFRACTION (2.4 Å)