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- EMDB-45507: In situ structure of C. jejuni flagellar motor -

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Basic information

Entry
Database: EMDB / ID: EMD-45507
TitleIn situ structure of C. jejuni flagellar motor
Map dataIn situ structure of C. jejuni flagellar motor
Sample
  • Cell: Campylobacter jejuni
KeywordsC. jejuni / Flagella / Complex / Flagellar motor / MOTOR PROTEIN
Biological speciesCampylobacter jejuni (Campylobacter)
Methodsubtomogram averaging / cryo EM / Resolution: 29.2 Å
AuthorsTachiyama S / Zhao H / Liu J
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Proc Natl Acad Sci U S A / Year: 2025
Title: Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility in .
Authors: Yuanyuan Chen / Shoichi Tachiyama / Yuqian Li / Xueyin Feng / Hang Zhao / Yanmin Wu / Yu Guo / María Lara-Tejero / Canfeng Hua / Jun Liu / Beile Gao /
Abstract: Rotation of the bacterial flagellum, the first identified biological rotary machine, is driven by its stator units. Knowledge gained about the function of stator units has increasingly led to studies ...Rotation of the bacterial flagellum, the first identified biological rotary machine, is driven by its stator units. Knowledge gained about the function of stator units has increasingly led to studies of rotary complexes in different cellular pathways. Here, we report that a tetrameric PilZ family protein, FlgX, is a structural component underneath the stator units in the flagellar motor of . FlgX forms a stable tetramer that does not bind cyclic di-GMP (c-di-GMP), unlike other canonical PilZ domain-containing proteins. Cryoelectron tomography and subtomogram averaging of flagellar motors in situ provide evidence that FlgX interacts with each stator unit and plays a critical role in stator ring assembly and stability. Furthermore, FlgX is conserved and was most likely present in the common ancestor of the phylum . Overall, FlgX represents a divergence in function for PilZ superfamily proteins as well as a player in the key stator-rotor interaction of complex flagellar motors.
History
DepositionJun 26, 2024-
Header (metadata) releaseJun 4, 2025-
Map releaseJun 4, 2025-
UpdateJun 4, 2025-
Current statusJun 4, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_45507.png

Downloads & links

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Map

FileDownload / File: emd_45507.map.gz / Format: CCP4 / Size: 59.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationIn situ structure of C. jejuni flagellar motor
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
4.3 Å/pix.
x 250 pix.
= 1074. Å		4.3 Å/pix.
x 250 pix.
= 1074. Å		4.3 Å/pix.
x 250 pix.
= 1074. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 4.296 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0764
Minimum - Maximum-0.56419784 - 0.7189934
Average (Standard dev.)0.00000000000173 (±0.07896255)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions250250250
Spacing250250250
CellA=B=C: 1074.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half map of C. jejuni flagellar motor structure

Fileemd_45507_half_map_1.map
AnnotationHalf map of C. jejuni flagellar motor structure
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map of C. jejuni flagellar motor structure

Fileemd_45507_half_map_2.map
AnnotationHalf map of C. jejuni flagellar motor structure
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Campylobacter jejuni

EntireName: Campylobacter jejuni (Campylobacter)
Components
  • Cell: Campylobacter jejuni

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Supramolecule #1: Campylobacter jejuni

SupramoleculeName: Campylobacter jejuni / type: cell / ID: 1 / Parent: 0
Source (natural)Organism: Campylobacter jejuni (Campylobacter)

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Experimental details

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Structure determination

Methodcryo EM
Processingsubtomogram averaging
Aggregation statecell

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE-PROPANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 1.96 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 5.0 µm / Nominal defocus min: 3.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: C17 (17 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 29.2 Å / Resolution method: FSC 0.5 CUT-OFF / Number subtomograms used: 4454
ExtractionNumber tomograms: 216 / Number images used: 262
CTF correctionType: PHASE FLIPPING ONLY
Final angle assignmentType: OTHER

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