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BACTERIAL FLAGELLUM

Hooked on motility

Nature Structural & Molecular Biology volume 26, pages 848–849 (2019)Cite this article

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A new cryo-EM structure of the bacterial flagellar hook, which connects the motor to the flagellar filament, reveals 11 distinctive conformations of the subunit. The cooperative dynamic switching among these states offers a dramatic extension of two-state models of protein allostery.

Although initial observations of bacterial motility date from the time of Leeuwenhoek in the 17th century, bacterial motility driven by the flagellar system has been under intense study in the ‘modern era’ for more than 50 years. The bacterial flagellar system has no homology to the eukaryotic one, which drives the motility of cells ranging from trypanosomes to mammalian sperm. The two systems function by entirely different mechanisms (that is, bacterial flagella rotate1 whereas the eukaryotic ones beat2), but both form whip-like tails that propel cells. Between the flagellar motor, located within the bacterial cell, and the extracellular flagellar filament there exists a structure called the flagellar hook, which is polymerized from a single protein (FlgE in Salmonella species). The hook acts as a universal joint, allowing the flagellar filament to be oriented in different directions, including parallel to the cell surface, while it is still rotating. A new structure of the hook by Shibata et al. not only is a technical tour de force of cryo-EM but also provides many insights into everything from flagellar motility to protein allostery3.

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Fig. 1: A view down the curved lumen of the supercoiled flagellar hook.

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  1. Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA

    Edward H. Egelman

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  1. Edward H. Egelman
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Correspondence to Edward H. Egelman.

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Egelman, E.H. Hooked on motility. Nat Struct Mol Biol 26, 848–849 (2019). https://doi.org/10.1038/s41594-019-0302-2

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