Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Convergent evolution in the supercoiling of prokaryotic flagellar filaments.
Journal, issue, pages	Cell, Vol. 185, Issue 19, Page 3487-3500.e14, Year 2022
Publish date	Sep 15, 2022
Authors	Mark 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 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 ...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 links	Cell / PubMed:36057255 / PubMed Central
Methods	EM (helical sym.) / EM (single particle)
Resolution	2.9 - 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 27008 8cvi 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 27026 8cwm 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 27060 8cxm 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 27076 8cye 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)
Keywords	STRUCTURAL PROTEIN / Bacterial motility / flagellar filament / flagellin / Archaea / Motility / supercoiling / Bacterial flagellum