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8CVI

Cryo-EM structure of the supercoiled EPEC H6 flagellar filament core Curly I waveform

Summary for 8CVI
Entry DOI10.2210/pdb8cvi/pdb
EMDB information27008
DescriptorFlagellin (1 entity in total)
Functional Keywordsbacterial motility, flagellar filament, flagellin, structural protein
Biological sourceEscherichia coli
Total number of polymer chains33
Total formula weight1859286.26
Authors
Kreutzberger, M.A.,Chatterjee, S.,Frankel, G.,Egelman, E.H. (deposition date: 2022-05-18, release date: 2022-09-07, Last modification date: 2024-06-12)
Primary citationKreutzberger, 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.
Convergent evolution in the supercoiling of prokaryotic flagellar filaments.
Cell, 185:3487-3500.e14, 2022
Cited by
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.
PubMed: 36057255
DOI: 10.1016/j.cell.2022.08.009
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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건을2024-11-06부터공개중

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