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''' | + | {{Structure |
| + | |PDB= 1io1 |SIZE=350|CAPTION= <scene name='initialview01'>1io1</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IO1 is a [ | + | 1IO1 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11268201 11268201] |
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: flagellin]] | [[Category: flagellin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:52:45 2008'' |
Revision as of 09:52, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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