7sn9
From Proteopedia
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<StructureSection load='7sn9' size='340' side='right'caption='[[7sn9]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='7sn9' size='340' side='right'caption='[[7sn9]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SN9 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=7sn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sn9 OCA], [https://pdbe.org/7sn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sn9 RCSB], [https://www.ebi.ac.uk/pdbsum/7sn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sn9 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]] 3.5Å</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=7sn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sn9 OCA], [https://pdbe.org/7sn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sn9 RCSB], [https://www.ebi.ac.uk/pdbsum/7sn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sn9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | == Function == | ||
- | [[https://www.uniprot.org/uniprot/FLAA_RHIML FLAA_RHIML]] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. Homomer of FlaA is able to form a functional filament. | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Flagellar filaments function as the propellers of the bacterial flagellum and their supercoiling is key to motility. The outer domains on the surface of the filament are non-critical for motility in many bacteria and their structures and functions are not conserved. Here, we show the atomic cryo-electron microscopy structures for flagellar filaments from enterohemorrhagic Escherichia coli O157:H7, enteropathogenic E. coli O127:H6, Achromobacter, and Sinorhizobium meliloti, where the outer domains dimerize or tetramerize to form either a sheath or a screw-like surface. These dimers are formed by 180 degrees rotations of half of the outer domains. The outer domain sheath (ODS) plays a role in bacterial motility by stabilizing an intermediate waveform and prolonging the tumbling of E. coli cells. Bacteria with these ODS and screw-like flagellar filaments are commonly found in soil and human intestinal environments of relatively high viscosity suggesting a role for the dimerization in these environments. | ||
- | + | ==See Also== | |
- | + | *[[Flagellin 3D structures|Flagellin 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Egelman | + | [[Category: Egelman EH]] |
- | [[Category: Kreutzberger | + | [[Category: Kreutzberger MAB]] |
- | [[Category: Scharf | + | [[Category: Scharf BE]] |
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Current revision
Cryo-EM structure of the Sinorhizobium meliloti flagellar filament
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