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TitleStructure of the bacterial flagellar protofilament and implications for a switch for supercoiling.
Journal, issue, pagesNature, Vol. 410, Issue 6826, Page 331-337, Year 2001
Publish dateMar 15, 2001
AuthorsF A Samatey / K Imada / S Nagashima / F Vonderviszt / T Kumasaka / M Yamamoto / K Namba /
PubMed AbstractThe 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 ...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.
External linksNature / PubMed:11268201
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-1io1:
CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN
Method: X-RAY DIFFRACTION / Resolution: 2.0 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • salmonella typhimurium (bacteria)
KeywordsSTRUCTURAL PROTEIN / beta-folium / flagellin

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