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1io1
From Proteopedia
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[[Image:1io1.gif|left|200px]] | [[Image:1io1.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN''' | '''CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN''' | ||
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[[Category: Vondervisz, F.]] | [[Category: Vondervisz, F.]] | ||
[[Category: Yamamoto, M.]] | [[Category: Yamamoto, M.]] | ||
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| - | [[Category: | + | [[Category: Flagellin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:12:20 2008'' | |
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Revision as of 17:12, 2 May 2008
CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN
Overview
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.
About this Structure
1IO1 is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 20:12:20 2008
