1IO1

CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN

Summary for 1IO1

• Entry DOI: 10.2210/pdb1io1/pdb
• Descriptor: PHASE 1 FLAGELLIN (2 entities in total)
• Functional Keywords: beta-folium, flagellin, structural protein
• Biological source: Salmonella typhimurium
• Cellular location: Secreted: P06179
• Total number of polymer chains: 1
• Total formula weight: 41351.97

Authors

Samatey, F.A.,Imada, K.,Nagashima, S.,Vondervisz, F.,Kumasaka, T.,Yamamoto, M.,Namba, K. (deposition date: 2000-12-28, release date: 2001-04-04, Last modification date: 2023-12-27)

Primary citation

Samatey, F.A.,Imada, K.,Nagashima, S.,Vondervisz, F.,Kumasaka, T.,Yamamoto, M.,Namba, K.
Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling
Nature, 410:331-337, 2001

PubMed 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.

PubMed: 11268201
DOI: 10.1038/35066504

Experimental method

X-RAY DIFFRACTION (2 Å)