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- EMDB-27076: Cryo-EM asymmetric reconstruction of the EPEC H6 bacterial flagel... -

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Basic information

Entry
Database: EMDB / ID: EMD-27076
TitleCryo-EM asymmetric reconstruction of the EPEC H6 bacterial flagellar filament Normal Waveform
Map data
Sample
  • Complex: Bacterial flagellar filaments
    • Protein or peptide: Flagellin
KeywordsBacterial flagellum / flagellin / bacterial motility / supercoiling / STRUCTURAL PROTEIN
Function / homology
Function and homology information


bacterial-type flagellum / structural molecule activity / extracellular region
Similarity search - Function
Flagellin, H7-serospecific domain / Flagellin protein / Flagellin, C-terminal domain, subdomain 2 / Flagellin, C-terminal domain / Bacterial flagellin C-terminal helical region / Flagellin / Flagellin, N-terminal domain / Bacterial flagellin N-terminal helical region
Similarity search - Domain/homology
Biological speciesEscherichia coli O127:H6 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsKreutzberger MAB / Chatterjee S / Frankel G / Egelman EH
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM122510 United States
CitationJournal: Cell / Year: 2022
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
DepositionMay 23, 2022-
Header (metadata) releaseSep 7, 2022-
Map releaseSep 7, 2022-
UpdateJun 4, 2025-
Current statusJun 4, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_27076.png

Downloads & links

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Map

FileDownload / File: emd_27076.map.gz / Format: CCP4 / Size: 926.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 624 pix.
= 673.92 Å		1.08 Å/pix.
x 624 pix.
= 673.92 Å		1.08 Å/pix.
x 624 pix.
= 673.92 Å

Surface

Projections

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.08 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.177
Minimum - Maximum-0.47394964 - 0.7790674
Average (Standard dev.)0.0014131576 (±0.021924425)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions624624624
Spacing624624624
CellA=B=C: 673.92004 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_27076_msk_1.map
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Half map: #2

Fileemd_27076_half_map_1.map
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Half map: #1

Fileemd_27076_half_map_2.map
Projections & Slices
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Histogram (log scale)

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Sample components

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Entire : Bacterial flagellar filaments

EntireName: Bacterial flagellar filaments
Components
  • Complex: Bacterial flagellar filaments
    • Protein or peptide: Flagellin

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Supramolecule #1: Bacterial flagellar filaments

SupramoleculeName: Bacterial flagellar filaments / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Escherichia coli O127:H6 (bacteria) / Strain: O127:H6

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Macromolecule #1: Flagellin

MacromoleculeName: Flagellin / type: protein_or_peptide / ID: 1 / Number of copies: 22 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli O127:H6 (bacteria)
Molecular weightTheoretical: 56.342008 KDa
SequenceString: 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

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination 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

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: EMDB MAP
EMDB ID:

27064

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.33 CUT-OFF / Number images used: 46895
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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