Related Experiment Video
Updated: Jan 3, 2026

Biophysical Characterization of Flagellar Motor Functions
Published on: January 18, 2017
Structure of the native supercoiled flagellar hook as a universal joint
Takayuki Kato1,2, Fumiaki Makino1,3, Tomoko Miyata1
1Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Abstract:
The Bacterial flagellar hook is a short supercoiled tubular structure made from a helical assembly of the hook protein FlgE. The hook acts as a universal joint that connects the flagellar basal body and filament, and smoothly transmits torque generated by the rotary motor to the helical filament propeller. In peritrichously flagellated bacteria, the hook allows the filaments to form a bundle behind the cell for swimming, and for the bundle to fall apart for tumbling. Here we report a native supercoiled hook structure at 3.6 Å resolution by cryoEM single particle image analysis of the polyhook. The atomic model built into the three-dimensional (3D) density map reveals the changes in subunit conformation and intersubunit interactions that occur upon compression and extension of the 11 protofilaments during their smoke ring-like rotation. These observations reveal how the hook functions as a dynamic molecular universal joint with high bending flexibility and twisting rigidity.
More Related Videos
Related Concept Videos
Flagella and Motility in Bacteria
Microtubules in Cell Motility
The Structure of Intermediate Filaments
Intermediate...
Fimbriae, Pili, and Axial Filaments
Generation of Straight or Branched Actin Filaments
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
ATP Synthase: Structure

