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- EMDB-26995: Cryo-EM helical reconstruction of the EPEC H6 Curly I flagellar core -
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Open data
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Basic information
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Title | Cryo-EM helical reconstruction of the EPEC H6 Curly I flagellar core | |||||||||
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Biological species | ![]() ![]() ![]() | |||||||||
Method | helical reconstruction / ![]() | |||||||||
![]() | Kreutzberger MAB / Chatterjee S / Frankel G / Egelman EH | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Convergent evolution in the supercoiling of prokaryotic flagellar filaments. 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 / ...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 / ![]() ![]() ![]() 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. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 22.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.7 KB 13.7 KB | Display Display | ![]() |
Images | ![]() | 43.9 KB | ||
Masks | ![]() | 216 MB | ![]() | |
Others | ![]() ![]() | 198.8 MB 198.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
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Voxel size | X=Y=Z: 1.08 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_26995_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_26995_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Bacterial flagellar filament core
Entire | Name: Bacterial flagellar filament core |
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Components |
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-Supramolecule #1: Bacterial flagellar filament core
Supramolecule | Name: Bacterial flagellar filament core / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() ![]() |
-Macromolecule #1: Bacterial flagellin
Macromolecule | Name: Bacterial flagellin / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() ![]() |
Sequence | String: MAQVINTNSL SLITQNNINK NQSALSSSIE RLSSGLRINS AKDDAAGQAI ANRFTSNIKG LTQAARNAN DGISVAQTTE GALSEINNNL QRIRELTVQA STGTNSDSDL DSIQDEIKSR L DEIDRVSG QTQFNGVNVL AKDGSMKIQV GANDGQTITI DLKKIDSDTL ...String: MAQVINTNSL SLITQNNINK NQSALSSSIE RLSSGLRINS AKDDAAGQAI ANRFTSNIKG LTQAARNAN DGISVAQTTE GALSEINNNL QRIRELTVQA STGTNSDSDL DSIQDEIKSR L DEIDRVSG QTQFNGVNVL AKDGSMKIQV GANDGQTITI DLKKIDSDTL GLNGFNVNGK GE TANTAAT LKDMSGFTAA AAPGGTVGVT QYTDKSAVAS SVDILNAVAG ADGNKVTTSA DVG FGTPAA AVTYTYNKDT NSYSAASDDI SSANLAAFLN PQARDTTKAT VTIGGKDQDV NIDK SGNLT AADDGAVLYM DATGNLTKNN AGGDTQATLA KVATATGAKA ATIQTDKGTF TSDGT AFDG ASMSIDANTF ANAVKNDTYT ATVGAKTYSV TTGSAAADTA YMSNGVLSDT PPTYYA QAD GSITTTEDAA AGKLVYKGSD GKLTTDTTSK AESTSDPLAA LDDAISQIDK FRSSLGA VQ NRLDSAVTNL NNTTTNLSEA QSRIQDADYA TEVSNMSKAQ IIQQAGNSVL AKANQVPQ Q VLSLLQG |
-Experimental details
-Structure determination
Method | ![]() |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 6.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: EMDB MAP EMDB ID: |
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Final angle assignment | Type: NOT APPLICABLE |
Final reconstruction | Applied symmetry - Helical parameters - Δz: 4.813 Å Applied symmetry - Helical parameters - Δ&Phi: 65.539 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 269269 |