Structure of the native supercoiled flagellar hook as a universal joint

Takayuki Kato, Fumiaki Makino, Tomoko Miyata, Peter Horváth and Keiichi Namba

Aug 30, 2019
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Received Date: 23rd August 19

Bacteria swim in viscous liquid environments by using the flagellum1-3. The flagellum is composed of about 30 different proteins and can be roughly divided into three parts: the basal body, the hook and the filament. The basal body acts as a rotary motor powered by ion motive force across the cytoplasmic membrane as well as a protein export apparatus to construct the axial structure of the flagellum. The filament is as a helical propeller, and it is a supercoiled form of a helical tubular assembly consisting of a few tens of thousands of flagellin molecules4. The hook is a relatively short axial segment working as a universal joint connecting the basal body and the filament for smooth transmission of motor torque to the filament5,6. The structure of hook has been studied by combining X-ray crystal structure of a core fragment of hook protein FlgE and electron cryomicroscopy (cryoEM) helical image analysis of the polyhook in the straight form and has given a deep insight into the universal joint mechanism7. However, the supercoiled structure of the hook was an approximate model based on the atomic model of the straight hook without its inner core domain7 and EM observations of supercoiled polyhook by freeze-dry and Pt/Pd shadow cast8. Here we report the native supercoiled hook structure at 3.1 Å resolution by cryoEM single particle image analysis of the polyhook. The atomic model built on the three-dimensional (3D) density map show the actual changes in subunit conformation and intersubunit interactions upon compression and extension of the 11 protofilaments that occur during their smoke ring-like rotation and allow the hook to function as a dynamic molecular universal joint with high bending flexibility and twisting rigidity.

Read in full at bioRxiv.

This is an abstract of a preprint hosted on an independent third party site. It has not been peer reviewed but is currently under consideration at Nature Communications.

Nature Communications

Nature Research, Springer Nature