3a5x: Difference between revisions

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<SX load='3a5x' size='340' side='right' viewer='molstar' caption='[[3a5x]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
<SX load='3a5x' size='340' side='right' viewer='molstar' caption='[[3a5x]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3a5x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A5X FirstGlance]. <br>
<table><tr><td colspan='2'>[[3a5x]] 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=3A5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A5X FirstGlance]. <br>
</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=3a5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5x OCA], [https://pdbe.org/3a5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a5x RCSB], [https://www.ebi.ac.uk/pdbsum/3a5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a5x ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</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=3a5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5x OCA], [https://pdbe.org/3a5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a5x RCSB], [https://www.ebi.ac.uk/pdbsum/3a5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a5x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FLIC_SALTY FLIC_SALTY]] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=3a5x ConSurf].
</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=3a5x ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The bacterial flagellar filament is a helical propeller rotated by the flagellar motor for bacterial locomotion. The filament is a supercoiled assembly of a single protein, flagellin, and is formed by 11 protofilaments. For bacterial taxis, the reversal of motor rotation switches the supercoil between left- and right-handed, both of which arise from combinations of two distinct conformations and packing interactions of the L-type and R-type protofilaments. Here we report an atomic model of the L-type straight filament by electron cryomicroscopy and helical image analysis. Comparison with the R-type structure shows interesting features: an orientation change of the outer core domains (D1) against the inner core domains (D0) showing almost invariant orientation and packing, a conformational switching within domain D1, and the conformational flexibility of domains D0 and D1 with their spoke-like connection for tight molecular packing.
Conformational change of flagellin for polymorphic supercoiling of the flagellar filament.,Maki-Yonekura S, Yonekura K, Namba K Nat Struct Mol Biol. 2010 Apr;17(4):417-22. Epub 2010 Mar 14. PMID:20228803<ref>PMID:20228803</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3a5x" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Flagellin 3D structures|Flagellin 3D structures]]
*[[Flagellin 3D structures|Flagellin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Salmonella typhimurium]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Maki-Yonekura, S]]
[[Category: Maki-Yonekura S]]
[[Category: Namba, K]]
[[Category: Namba K]]
[[Category: Yonekura, K]]
[[Category: Yonekura K]]
[[Category: Bacterial flagellum]]
[[Category: Flagellar filament]]
[[Category: Flagellin]]
[[Category: Helical reconstruction]]
[[Category: Motor protein]]
[[Category: Secreted]]
[[Category: Structural protein]]

Latest revision as of 13:59, 13 March 2024

L-type straight flagellar filament made of full-length flagellin

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