3A69

Atomic model of the bacterial flagellar hook based on docking an X-ray derived structure and terminal two alpha-helices into an 7.1 angstrom resolution cryoEM map

3A69 の概要

• エントリーDOI: 10.2210/pdb3a69/pdb
• EMDBエントリー: 1647
• 分子名称: Flagellar hook protein flgE (1 entity in total)
• 機能のキーワード: the bacterial flagellar motor, universal joint, bacterial flagellum, motor protein
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42101.96

構造登録者

Fujii, T.,Kato, T.,Namba, K. (登録日: 2009-08-26, 公開日: 2009-12-15, 最終更新日: 2024-03-13)

主引用文献

Fujii, T.,Kato, T.,Namba, K.
Specific arrangement of alpha-helical coiled coils in the core domain of the bacterial flagellar hook for the universal joint function
Structure, 17:1485-1493, 2009

PubMed Abstract: The bacterial flagellar hook is a short, highly curved tubular structure connecting the rotary motor to the filament acting as a helical propeller. The bending flexibility of the hook allows it to work as a universal joint. A partial atomic model of the hook revealed a sliding intersubunit domain interaction along the protofilament to produce bending flexibility. However, it remained unclear how the tightly packed inner core domains can still permit axial extension and compression. We report advances in cryoEM image analysis for high-resolution, high-throughput structural analysis and a density map of the hook that reveals most of the secondary structures, including the terminal alpha helices forming a coiled coil. The orientations and axial packing interactions of these two alpha helices are distinctly different from those of the filament, allowing them to have a room for axial compression and extension for bending flexibility without impairing the mechanical stability of the hook.

PubMed: 19913483
DOI: 10.1016/j.str.2009.08.017

実験手法

ELECTRON MICROSCOPY (7.1 Å)