3a69
From Proteopedia
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==Atomic model of the bacterial flagellar hook based on docking an X-ray derived structure and terminal two alpha-helices into an 7.1 angstrom resolution cryoEM map== | ==Atomic model of the bacterial flagellar hook based on docking an X-ray derived structure and terminal two alpha-helices into an 7.1 angstrom resolution cryoEM map== | ||
| - | < | + | <SX load='3a69' size='340' side='right' viewer='molstar' caption='[[3a69]], [[Resolution|resolution]] 7.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3a69]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3a69]] 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=3A69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A69 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.1Å</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=3a69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a69 OCA], [https://pdbe.org/3a69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a69 RCSB], [https://www.ebi.ac.uk/pdbsum/3a69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a69 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FLGE_SALTY FLGE_SALTY] | ||
== 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=3a69 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=3a69 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The bacterial flagellar hook is a short, highly curved tubular structure connecting the rotary motor to the filament acting as a helical propeller. The bending flexibility of the hook allows it to work as a universal joint. A partial atomic model of the hook revealed a sliding intersubunit domain interaction along the protofilament to produce bending flexibility. However, it remained unclear how the tightly packed inner core domains can still permit axial extension and compression. We report advances in cryoEM image analysis for high-resolution, high-throughput structural analysis and a density map of the hook that reveals most of the secondary structures, including the terminal alpha helices forming a coiled coil. The orientations and axial packing interactions of these two alpha helices are distinctly different from those of the filament, allowing them to have a room for axial compression and extension for bending flexibility without impairing the mechanical stability of the hook. | ||
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| - | Specific arrangement of alpha-helical coiled coils in the core domain of the bacterial flagellar hook for the universal joint function.,Fujii T, Kato T, Namba K Structure. 2009 Nov 11;17(11):1485-93. PMID:19913483<ref>PMID:19913483</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3a69" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Flagellar protein|Flagellar protein]] | + | *[[Flagellar protein 3D structures|Flagellar protein 3D structures]] |
*[[The Bacterial Flagellar Hook|The Bacterial Flagellar Hook]] | *[[The Bacterial Flagellar Hook|The Bacterial Flagellar Hook]] | ||
| - | *[[User:Fadel A. Samatey/FlgE III/Intrinsically Disordered Flagellar Rod Stretch|User:Fadel A. Samatey/FlgE III/Intrinsically Disordered Flagellar Rod Stretch]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
| - | [[Category: Salmonella enterica subsp. enterica serovar | + | [[Category: Large Structures]] |
| - | [[Category: Fujii | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
| - | [[Category: Kato | + | [[Category: Fujii T]] |
| - | [[Category: Namba | + | [[Category: Kato T]] |
| - | + | [[Category: Namba K]] | |
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Current revision
Atomic model of the bacterial flagellar hook based on docking an X-ray derived structure and terminal two alpha-helices into an 7.1 angstrom resolution cryoEM map
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