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| | <SX load='5wjt' size='340' side='right' viewer='molstar' caption='[[5wjt]], [[Resolution|resolution]] 3.80Å' scene=''> | | <SX load='5wjt' size='340' side='right' viewer='molstar' caption='[[5wjt]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wjt]] is a 41 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WJT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WJT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wjt]] is a 41 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WJT FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B4417_3365 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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]] 3.8Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5wjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wjt OCA], [http://pdbe.org/5wjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wjt RCSB], [http://www.ebi.ac.uk/pdbsum/5wjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wjt ProSAT]</span></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=5wjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wjt OCA], [https://pdbe.org/5wjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wjt RCSB], [https://www.ebi.ac.uk/pdbsum/5wjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wjt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A162QQD4_BACIU A0A162QQD4_BACIU]] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.[RuleBase:RU362073] | + | [https://www.uniprot.org/uniprot/FLA_BACSU FLA_BACSU] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The bacterial flagellar filament has long been studied to understand how a polymer composed of a single protein can switch between different supercoiled states with high cooperativity. Here we present near-atomic resolution cryo-EM structures for flagellar filaments from both Gram-positive Bacillus subtilis and Gram-negative Pseudomonas aeruginosa. Seven mutant flagellar filaments in B. subtilis and two in P. aeruginosa capture two different states of the filament. These reliable atomic models of both states reveal conserved molecular interactions in the interior of the filament among B. subtilis, P. aeruginosa and Salmonella enterica. Using the detailed information about the molecular interactions in two filament states, we successfully predict point mutations that shift the equilibrium between those two states. Further, we observe the dimerization of P. aeruginosa outer domains without any perturbation of the conserved interior of the filament. Our results give new insights into how the flagellin sequence has been "tuned" over evolution.Bacterial flagellar filaments are composed almost entirely of a single protein-flagellin-which can switch between different supercoiled states in a highly cooperative manner. Here the authors present near-atomic resolution cryo-EM structures of nine flagellar filaments, and begin to shed light on the molecular basis of filament switching.
| + | |
| - | | + | |
| - | A structural model of flagellar filament switching across multiple bacterial species.,Wang F, Burrage AM, Postel S, Clark RE, Orlova A, Sundberg EJ, Kearns DB, Egelman EH Nat Commun. 2017 Oct 16;8(1):960. doi: 10.1038/s41467-017-01075-5. PMID:29038601<ref>PMID:29038601</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5wjt" 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: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Burrage, A M]] | + | [[Category: Burrage AM]] |
| - | [[Category: Egelman, E H]] | + | [[Category: Egelman EH]] |
| - | [[Category: Kearns, D B]] | + | [[Category: Kearns DB]] |
| - | [[Category: Wang, F]] | + | [[Category: Wang F]] |
| - | [[Category: Bacteria flagella]]
| + | |
| - | [[Category: Cryo-em]]
| + | |
| - | [[Category: Helical polymer]]
| + | |
| - | [[Category: Protein fibril]]
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