1io1: Difference between revisions

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[[Image:1io1.gif|left|200px]]
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{{STRUCTURE_1io1|  PDB=1io1  |  SCENE=  }}  
{{STRUCTURE_1io1|  PDB=1io1  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN'''
===CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11268201}}


==About this Structure==
==About this Structure==
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[[Category: Beta-folium]]
[[Category: Beta-folium]]
[[Category: Flagellin]]
[[Category: Flagellin]]
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Revision as of 10:38, 1 July 2008

File:1io1.png

Template:STRUCTURE 1io1

CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN

Template:ABSTRACT PUBMED 11268201

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

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