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1io1
From Proteopedia
| 1io1, resolution 2.00Å () | |||||||||
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| Domains: | Flagellin_N, Flagellin_D3, PRK08869, Flagellin_C | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN
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.
Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling., Samatey FA, Imada K, Nagashima S, Vonderviszt F, Kumasaka T, Yamamoto M, Namba K, Nature. 2001 Mar 15;410(6826):331-7. PMID:11268201
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1IO1 is a 1 chain structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
- Samatey FA, Imada K, Nagashima S, Vonderviszt F, Kumasaka T, Yamamoto M, Namba K. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature. 2001 Mar 15;410(6826):331-7. PMID:11268201
Page seeded by OCA on Tue Feb 17 13:41:08 2009
