Abstract
The bacterial flagellar filament is a helical propeller constructed from 11 protofilaments of a single protein, flagellin. The filament switches between left- and right-handed supercoiled forms when bacteria switch their swimming mode between running and tumbling. Supercoiling is produced by two different packing interactions of flagellin called L and R. In switching from L to R, the intersubunit distance (∼52 Å) along the protofilament decreases by 0.8 Å. Changes in the number of L and R protofilaments govern supercoiling of the filament. Here we report the 2.0 Å resolution crystal structure of a Salmonella flagellin fragment of relative molecular mass 41,300. The crystal contains pairs of antiparallel straight protofilaments with the R-type repeat. By simulated extension of the protofilament model, we have identified possible switch regions responsible for the bi-stable mechanical switch that generates the 0.8 Å difference in repeat distance.
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Acknowledgements
We thank T. Tomizaki, L. Dumon, W. Burmeister, S. Arzt and S. Wakatsuki at ESRF, and M. Kawamoto, N. Kamiya and K. Miura at SPring-8 for technical help with beamlines. We also thank I. Yamashita and K. Hasegawa for a mutant strain of Salmonella that produces SJW1655-derived site-directed mutant flagellin (G365C), which forms the R-type straight flagellar filament, and helpful information of heavy-atom binding to the filament; J. Tame for critically reading the manuscript; and S. Asakura, T. Nitta and F. Oosawa for continuous support and encouragement.
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Samatey, F., Imada, K., Nagashima, S. et al. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature 410, 331–337 (2001). https://doi.org/10.1038/35066504
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DOI: https://doi.org/10.1038/35066504
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