1io1: Difference between revisions

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New page: left|200px<br /><applet load="1io1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1io1, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1io1.gif|left|200px]]<br /><applet load="1io1" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1io1.gif|left|200px]]<br /><applet load="1io1" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1io1, resolution 2.0&Aring;" />
caption="1io1, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN'''<br />
'''CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN'''<br />


==Overview==
==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.
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==
==About this Structure==
1IO1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IO1 OCA].  
1IO1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO1 OCA].  


==Reference==
==Reference==
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[[Category: Nagashima, S.]]
[[Category: Nagashima, S.]]
[[Category: Namba, K.]]
[[Category: Namba, K.]]
[[Category: Samatey, F.A.]]
[[Category: Samatey, F A.]]
[[Category: Vondervisz, F.]]
[[Category: Vondervisz, F.]]
[[Category: Yamamoto, M.]]
[[Category: Yamamoto, M.]]
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[[Category: flagellin]]
[[Category: flagellin]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:45 2008''

Revision as of 14:13, 21 February 2008

File:1io1.gif


1io1, resolution 2.0Å

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CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN

OverviewOverview

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 StructureAbout this Structure

1IO1 is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

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

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