Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling

Fadel A. Samatey, Katsumi Imada, Shigehiro Nagashima, Ferenc Vonderviszt, Takashi Kumasaka, Masaki Yamamoto and Keiichi Namba ()
Additional contact information
Fadel A. Samatey: Protonic NanoMachine Project, ERATO, JST
Katsumi Imada: Protonic NanoMachine Project, ERATO, JST
Shigehiro Nagashima: Protonic NanoMachine Project, ERATO, JST
Ferenc Vonderviszt: University of Veszprém
Takashi Kumasaka: RIKEN Harima Institute
Masaki Yamamoto: RIKEN Harima Institute
Keiichi Namba: Protonic NanoMachine Project, ERATO, JST

Nature, 2001, vol. 410, issue 6826, 331-337

Abstract: 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.

Date: 2001
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DOI: 10.1038/35066504

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