8CWM

Cryo-EM structure of the supercoiled S. islandicus REY15A archaeal flagellar filament


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.40 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Convergent evolution in the supercoiling of prokaryotic flagellar filaments.

Kreutzberger, M.A.B.Sonani, R.R.Liu, J.Chatterjee, S.Wang, F.Sebastian, A.L.Biswas, P.Ewing, C.Zheng, W.Poly, F.Frankel, G.Luisi, B.F.Calladine, C.R.Krupovic, M.Scharf, B.E.Egelman, E.H.

(2022) Cell 185: 3487-3500.e14

  • DOI: https://doi.org/10.1016/j.cell.2022.08.009
  • Primary Citation of Related Structures:  
    8CVI, 8CWM, 8CXM, 8CYE

  • PubMed Abstract: 

    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.


  • Organizational Affiliation

    Department of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, VA 22903, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Flagellin306Sulfolobus islandicus REY15AMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for F0NG73 (Sulfolobus islandicus (strain REY15A))
Explore F0NG73 
Go to UniProtKB:  F0NG73
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupF0NG73
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.40 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesGM122510

Revision History  (Full details and data files)

  • Version 1.0: 2022-09-07
    Type: Initial release
  • Version 1.1: 2022-09-14
    Changes: Database references
  • Version 1.2: 2022-09-28
    Changes: Database references