1io1
From Proteopedia
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| - | [[Image:1io1.gif|left|200px]]<br /><applet load="1io1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1io1, resolution 2.0Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN'''<br /> | ||
| - | == | + | ==CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN== |
| + | <StructureSection load='1io1' size='340' side='right'caption='[[1io1]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1io1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IO1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1io1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io1 OCA], [https://pdbe.org/1io1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1io1 RCSB], [https://www.ebi.ac.uk/pdbsum/1io1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1io1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FLIC_SALTY FLIC_SALTY] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/io/1io1_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1io1 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | ||
| - | + | 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<ref>PMID:11268201</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1io1" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Flagellar protein|Flagellar protein]] | ||
| + | *[[Flagellin 3D structures|Flagellin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] | ||
| + | [[Category: Imada K]] | ||
| + | [[Category: Kumasaka T]] | ||
| + | [[Category: Nagashima S]] | ||
| + | [[Category: Namba K]] | ||
| + | [[Category: Samatey FA]] | ||
| + | [[Category: Vondervisz F]] | ||
| + | [[Category: Yamamoto M]] | ||
Current revision
CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN
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