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- EMDB-27076: Cryo-EM asymmetric reconstruction of the EPEC H6 bacterial flagel... -
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Open data
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Basic information
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Title | Cryo-EM asymmetric reconstruction of the EPEC H6 bacterial flagellar filament Normal Waveform | |||||||||
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![]() | Bacterial flagellum / flagellin / bacterial motility / supercoiling / STRUCTURAL PROTEIN | |||||||||
Function / homology | ![]() bacterial-type flagellum / structural molecule activity / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.9 Å | |||||||||
![]() | 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 | ![]() | 70.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.8 KB 14.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 20.6 KB | Display | ![]() |
Images | ![]() | 25.8 KB | ||
Masks | ![]() | 926.9 MB | ![]() | |
Filedesc metadata | ![]() | 5.1 KB | ||
Others | ![]() ![]() | 859 MB 859.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 30 KB | Display | |
Data in CIF | ![]() | 39.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8cyeMC ![]() 8cviC ![]() 8cwmC ![]() 8cxmC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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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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Density Histograms |
-Half map: #2
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Density Histograms |
-Half map: #1
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Density Histograms |
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Sample components
-Entire : Bacterial flagellar filaments
Entire | Name: Bacterial flagellar filaments |
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Components |
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-Supramolecule #1: Bacterial flagellar filaments
Supramolecule | Name: Bacterial flagellar filaments / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Flagellin
Macromolecule | Name: Flagellin / type: protein_or_peptide / ID: 1 / Number of copies: 22 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 56.342008 KDa |
Sequence | String: MAQVINTNSL SLITQNNINK NQSALSSSIE RLSSGLRINS AKDDAAGQAI ANRFTSNIKG LTQAARNAND GISVAQTTEG ALSEINNNL QRIRELTVQA STGTNSDSDL DSIQDEIKSR LDEIDRVSGQ TQFNGVNVLA KDGSMKIQVG ANDGQTITID L KKIDSDTL ...String: MAQVINTNSL SLITQNNINK NQSALSSSIE RLSSGLRINS AKDDAAGQAI ANRFTSNIKG LTQAARNAND GISVAQTTEG ALSEINNNL QRIRELTVQA STGTNSDSDL DSIQDEIKSR LDEIDRVSGQ TQFNGVNVLA KDGSMKIQVG ANDGQTITID L KKIDSDTL GLNGFNVNGK GETANTAATL KDMSGFTAAA APGGTVGVTQ YTDKSAVASS VDILNAVAGA DGNKVTTSAD VG FGTPAAA VTYTYNKDTN SYSAASDDIS SANLAAFLNP QARDTTKATV TIGGKDQDVN IDKSGNLTAA DDGAVLYMDA TGN LTKNNA GGDTQATLAK VATATGAKAA TIQTDKGTFT SDGTAFDGAS MSIDANTFAN AVKNDTYTAT VGAKTYSVTT GSAA ADTAY MSNGVLSDTP PTYYAQADGS ITTTEDAAAG KLVYKGSDGK LTTDTTSKAE STSDPLAALD DAISQIDKFR SSLGA VQNR LDSAVTNLNN TTTNLSEAQS RIQDADYATE VSNMSKAQII QQAGNSVLAK ANQVPQQVLS LLQG UniProtKB: Flagellin |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |