1io1

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Revision as of 18:24, 20 November 2007 by OCA (talk | contribs) (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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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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