8cye: Difference between revisions
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The | ==Cryo-EM asymmetric reconstruction of the EPEC H6 bacterial flagellar filament Normal Waveform== | ||
<StructureSection load='8cye' size='340' side='right'caption='[[8cye]], [[Resolution|resolution]] 3.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8cye]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O127:H6 Escherichia coli O127:H6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CYE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CYE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9Å</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=8cye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cye OCA], [https://pdbe.org/8cye PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cye RCSB], [https://www.ebi.ac.uk/pdbsum/8cye PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cye ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FLIC_ECO27 FLIC_ECO27] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The supercoiling of bacterial and archaeal flagellar filaments is required for motility. Archaeal flagellar filaments have no homology to their bacterial counterparts and are instead homologs of bacterial type IV pili. How these prokaryotic flagellar filaments, each composed of thousands of copies of identical subunits, can form stable supercoils under torsional stress is a fascinating puzzle for which structural insights have been elusive. Advances in cryoelectron microscopy (cryo-EM) make it now possible to directly visualize the basis for supercoiling, and here, we show the atomic structures of supercoiled bacterial and archaeal flagellar filaments. For the bacterial flagellar filament, we identify 11 distinct protofilament conformations with three broad classes of inter-protomer interface. For the archaeal flagellar filament, 10 protofilaments form a supercoil geometry supported by 10 distinct conformations, with one inter-protomer discontinuity creating a seam inside of the curve. Our results suggest that convergent evolution has yielded stable superhelical geometries that enable microbial locomotion. | |||
Convergent evolution in the supercoiling of prokaryotic flagellar filaments.,Kreutzberger MAB, Sonani RR, Liu J, Chatterjee S, Wang F, Sebastian AL, Biswas P, Ewing C, Zheng W, Poly F, Frankel G, Luisi BF, Calladine CR, Krupovic M, Scharf BE, Egelman EH Cell. 2022 Sep 15;185(19):3487-3500.e14. doi: 10.1016/j.cell.2022.08.009. Epub , 2022 Sep 2. PMID:36057255<ref>PMID:36057255</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8cye" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Frankel | ==See Also== | ||
[[Category: Kreutzberger | *[[Flagellin 3D structures|Flagellin 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli O127:H6]] | |||
[[Category: Large Structures]] | |||
[[Category: Chatterjee S]] | |||
[[Category: Egelman EH]] | |||
[[Category: Frankel G]] | |||
[[Category: Kreutzberger MAB]] | |||
Latest revision as of 08:18, 12 June 2024
Cryo-EM asymmetric reconstruction of the EPEC H6 bacterial flagellar filament Normal WaveformCryo-EM asymmetric reconstruction of the EPEC H6 bacterial flagellar filament Normal Waveform
Structural highlights
FunctionFLIC_ECO27 Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. Publication Abstract from PubMedThe supercoiling of bacterial and archaeal flagellar filaments is required for motility. Archaeal flagellar filaments have no homology to their bacterial counterparts and are instead homologs of bacterial type IV pili. How these prokaryotic flagellar filaments, each composed of thousands of copies of identical subunits, can form stable supercoils under torsional stress is a fascinating puzzle for which structural insights have been elusive. Advances in cryoelectron microscopy (cryo-EM) make it now possible to directly visualize the basis for supercoiling, and here, we show the atomic structures of supercoiled bacterial and archaeal flagellar filaments. For the bacterial flagellar filament, we identify 11 distinct protofilament conformations with three broad classes of inter-protomer interface. For the archaeal flagellar filament, 10 protofilaments form a supercoil geometry supported by 10 distinct conformations, with one inter-protomer discontinuity creating a seam inside of the curve. Our results suggest that convergent evolution has yielded stable superhelical geometries that enable microbial locomotion. Convergent evolution in the supercoiling of prokaryotic flagellar filaments.,Kreutzberger MAB, Sonani RR, Liu J, Chatterjee S, Wang F, Sebastian AL, Biswas P, Ewing C, Zheng W, Poly F, Frankel G, Luisi BF, Calladine CR, Krupovic M, Scharf BE, Egelman EH Cell. 2022 Sep 15;185(19):3487-3500.e14. doi: 10.1016/j.cell.2022.08.009. Epub , 2022 Sep 2. PMID:36057255[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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