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Identical folds used for distinct mechanical functions of the bacterial flagellar rod and hook

Takashi Fujii, Takayuki Kato, Koichi D. Hiraoka, Tomoko Miyata, Tohru Minamino, Fabienne F. V. Chevance, Kelly T. Hughes and Keiichi Namba ()
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Takashi Fujii: Graduate School of Frontier Biosciences, Osaka University
Takayuki Kato: Graduate School of Frontier Biosciences, Osaka University
Koichi D. Hiraoka: Graduate School of Frontier Biosciences, Osaka University
Tomoko Miyata: Graduate School of Frontier Biosciences, Osaka University
Tohru Minamino: Graduate School of Frontier Biosciences, Osaka University
Fabienne F. V. Chevance: University of Utah
Kelly T. Hughes: University of Utah
Keiichi Namba: Graduate School of Frontier Biosciences, Osaka University

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: Abstract The bacterial flagellum is a motile organelle driven by a rotary motor, and its axial portions function as a drive shaft (rod), a universal joint (hook) and a helical propeller (filament). The rod and hook are directly connected to each other, with their subunit proteins FlgG and FlgE having 39% sequence identity, but show distinct mechanical properties; the rod is straight and rigid as a drive shaft whereas the hook is flexible in bending as a universal joint. Here we report the structure of the rod and comparison with that of the hook. While these two structures have the same helical symmetry and repeat distance and nearly identical folds of corresponding domains, the domain orientations differ by ∼7°, resulting in tight and loose axial subunit packing in the rod and hook, respectively, conferring the rigidity on the rod and flexibility on the hook. This provides a good example of versatile use of a protein structure in biological organisms.

Date: 2017
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DOI: 10.1038/ncomms14276

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