PMID:11268201
| Citation |
Samatey, FA, Imada, K, Nagashima, S, Vonderviszt, F, Kumasaka, T, Yamamoto, M and Namba, K (2001) Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature 410:331-7 |
|---|---|
| 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 ( approximately 52 A) along the protofilament decreases by 0.8 A. Changes in the number of L and R protofilaments govern supercoiling of the filament. Here we report the 2.0 A 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 A difference in repeat distance. |
| Links |
PubMed Online version:10.1038/35066504 |
| Keywords |
Crystallography, X-Ray; Flagellin/chemistry; Flagellin/genetics; Flagellin/metabolism; Models, Molecular; Molecular Motor Proteins; Mutation; Peptide Fragments/chemistry; Peptide Fragments/genetics; Peptide Fragments/metabolism; Protein Conformation; Protein Transport; Salmonella typhimurium/chemistry |
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