6K9Q

Structure of the native supercoiled hook as a universal joint

Summary for 6K9Q

• Entry DOI: 10.2210/pdb6k9q/pdb
• EMDB information: 9952
• Descriptor: Flagellar hook protein FlgE (1 entity in total)
• Functional Keywords: flagella motor, hook, native structure, supercoiled, flge, motor protein
• Biological source: Salmonella typhimurium (Salmonella enterica subsp. enterica serovar Typhimurium)
• Total number of polymer chains: 26
• Total formula weight: 1094650.88

Authors

Kato, T.,Miyata, T.,Makino, F.,Horvath, P.,Namba, K. (deposition date: 2019-06-17, release date: 2020-02-12, Last modification date: 2024-03-27)

Primary citation

Kato, T.,Makino, F.,Miyata, T.,Horvath, P.,Namba, K.
Structure of the native supercoiled flagellar hook as a universal joint.
Nat Commun, 10:5295-5295, 2019

PubMed 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.

PubMed: 31757961
DOI: 10.1038/s41467-019-13252-9

Experimental method

ELECTRON MICROSCOPY (3.1 Å)