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TitleConvergent evolution in the supercoiling of prokaryotic flagellar filaments.
Journal, issue, pagesCell, Vol. 185, Issue 19, Page 3487-3500.e14, Year 2022
Publish dateSep 15, 2022
AuthorsMark A B Kreutzberger / Ravi R Sonani / Junfeng Liu / Sharanya Chatterjee / Fengbin Wang / Amanda L Sebastian / Priyanka Biswas / Cheryl Ewing / Weili Zheng / Frédéric Poly / Gad Frankel / B F Luisi / Chris R Calladine / Mart Krupovic / Birgit E Scharf / Edward H Egelman /
PubMed AbstractThe 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 ...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.
External linksCell / PubMed:36057255 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution2.9 - 3.9 Å
Structure data

EMDB-26995: Cryo-EM helical reconstruction of the EPEC H6 Curly I flagellar core
Method: EM (helical sym.) / Resolution: 2.9 Å

EMDB-27008, PDB-8cvi:
Cryo-EM structure of the supercoiled EPEC H6 flagellar filament core Curly I waveform
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-27026, PDB-8cwm:
Cryo-EM structure of the supercoiled S. islandicus REY15A archaeal flagellar filament
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-27029: Longer Cryo-EM Density map of the EPEC H6 Curly I bacterial flagellar filament
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-27059: Cryo-EM structure of the helical E. coli K12 flagellar filament core
Method: EM (helical sym.) / Resolution: 3.0 Å

EMDB-27060, PDB-8cxm:
Cryo-EM structure of the supercoiled E. coli K12 flagellar filament core, Normal waveform
Method: EM (single particle) / Resolution: 3.21 Å

EMDB-27064: Cryo-EM Helical Reconstruction of the EPEC H6 flagellar filament in the Normal waveform
Method: EM (helical sym.) / Resolution: 3.1 Å

EMDB-27065: Cryo-EM helical reconstruction of the S. islandicus REY15A archaeal flagellar filament
Method: EM (helical sym.) / Resolution: 3.1 Å

EMDB-27076, PDB-8cye:
Cryo-EM asymmetric reconstruction of the EPEC H6 bacterial flagellar filament Normal Waveform
Method: EM (single particle) / Resolution: 3.9 Å

Source
  • escherichia coli (E. coli)
  • Sulfolobus islandicus (acidophilic)
  • sulfolobus islandicus rey15a (acidophilic)
  • escherichia coli k-12 (bacteria)
  • escherichia coli o127:h6 (bacteria)
KeywordsSTRUCTURAL PROTEIN / Bacterial motility / flagellar filament / flagellin / Archaea / Motility / supercoiling / Bacterial flagellum

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