8cvi: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8cvi]] is a 33 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CVI FirstGlance]. <br> | <table><tr><td colspan='2'>[[8cvi]] is a 33 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CVI 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=8cvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cvi OCA], [https://pdbe.org/8cvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cvi RCSB], [https://www.ebi.ac.uk/pdbsum/8cvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cvi 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]] 3.4Å</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=8cvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cvi OCA], [https://pdbe.org/8cvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cvi RCSB], [https://www.ebi.ac.uk/pdbsum/8cvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cvi ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == 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> | |||
</div> | |||
<div class="pdbe-citations 8cvi" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Flagellin 3D structures|Flagellin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 08:18, 12 June 2024
Cryo-EM structure of the supercoiled EPEC H6 flagellar filament core Curly I waveformCryo-EM structure of the supercoiled EPEC H6 flagellar filament core Curly I 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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