Specific arrangement of alpha-helical coiled coils in the core domain of the bacterial flagellar hook for the universal joint function.
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.
Fujii
Takashi
T
Dynamic NanoMachine Project, ICORP, JST, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.
Kato
Takayuki
T
Namba
Keiichi
K
D001426:Bacterial Proteins / Q000737:chemistry* / Q000648:ultrastructure; D020285:Cryoelectron Microscopy / Q000379:methods*; D005407:Flagella / Q000737:chemistry* / Q000648:ultrastructure; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000648:ultrastructure; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary / Q000235:genetics
D001426:Bacterial Proteins; D020409:Molecular Motor Proteins