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- EMDB-25704: Flagellar MS-complex of Helicobacter pylori fliP* -

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Basic information

Entry
Database: EMDB / ID: EMD-25704
TitleFlagellar MS-complex of Helicobacter pylori fliP*
Map dataFlagellar MS-complex of Helicobacter pylori fliP*
Sample
  • Cell: Flagellar MS-complex of Helicobacter pylori fliP*
Biological speciesHelicobacter pylori 26695 (bacteria)
Methodsubtomogram averaging / cryo EM / Resolution: 60.0 Å
AuthorsKaplan M / Oikonomou CM / Wood CR / Chreifi G / Subramanian P / Ortega DR / Chang YW / Beeby M / Shaffer LS / Jensen GJ
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI127401 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM130456 United States
CitationJournal: EMBO J / Year: 2022
Title: Novel transient cytoplasmic rings stabilize assembling bacterial flagellar motors.
Authors: Mohammed Kaplan / Catherine M Oikonomou / Cecily R Wood / Georges Chreifi / Poorna Subramanian / Davi R Ortega / Yi-Wei Chang / Morgan Beeby / Carrie L Shaffer / Grant J Jensen /
Abstract: The process by which bacterial cells build their intricate flagellar motility apparatuses has long fascinated scientists. Our understanding of this process comes mainly from studies of purified ...The process by which bacterial cells build their intricate flagellar motility apparatuses has long fascinated scientists. Our understanding of this process comes mainly from studies of purified flagella from two species, Escherichia coli and Salmonella enterica. Here, we used electron cryo-tomography (cryo-ET) to image the assembly of the flagellar motor in situ in diverse Proteobacteria: Hylemonella gracilis, Helicobacter pylori, Campylobacter jejuni, Pseudomonas aeruginosa, Pseudomonas fluorescens, and Shewanella oneidensis. Our results reveal the in situ structures of flagellar intermediates, beginning with the earliest flagellar type III secretion system core complex (fT3SScc) and MS-ring. In high-torque motors of Beta-, Gamma-, and Epsilon-proteobacteria, we discovered novel cytoplasmic rings that interact with the cytoplasmic torque ring formed by FliG. These rings, associated with the MS-ring, assemble very early and persist until the stators are recruited into their periplasmic ring; in their absence the stator ring does not assemble. By imaging mutants in Helicobacter pylori, we found that the fT3SScc proteins FliO and FliQ are required for the assembly of these novel cytoplasmic rings. Our results show that rather than a simple accretion of components, flagellar motor assembly is a dynamic process in which accessory components interact transiently to assist in building the complex nanomachine.
History
DepositionDec 13, 2021-
Header (metadata) releaseMay 25, 2022-
Map releaseMay 25, 2022-
UpdateJun 1, 2022-
Current statusJun 1, 2022Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_25704.png

Downloads & links

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Map

FileDownload / File: emd_25704.map.gz / Format: CCP4 / Size: 1.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFlagellar MS-complex of Helicobacter pylori fliP*
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
16.15 Å/pix.
x 70 pix.
= 1130.5 Å		16.15 Å/pix.
x 70 pix.
= 1130.5 Å		16.15 Å/pix.
x 70 pix.
= 1130.5 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 16.15 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 140.0
Minimum - Maximum-1.5258789e-05 - 255.0
Average (Standard dev.)108.183914 (±19.316877)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions707070
Spacing707070
CellA=B=C: 1130.5 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Flagellar MS-complex of Helicobacter pylori fliP*

EntireName: Flagellar MS-complex of Helicobacter pylori fliP*
Components
  • Cell: Flagellar MS-complex of Helicobacter pylori fliP*

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Supramolecule #1: Flagellar MS-complex of Helicobacter pylori fliP*

SupramoleculeName: Flagellar MS-complex of Helicobacter pylori fliP* / type: cell / ID: 1 / Parent: 0
Source (natural)Organism: Helicobacter pylori 26695 (bacteria)

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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 TECNAI F30
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 2.9 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 8.0 µm / Nominal defocus min: 6.0 µm
Experimental equipment
Model: Tecnai F30 / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 60.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number subtomograms used: 64
ExtractionNumber tomograms: 76 / Number images used: 64
Final angle assignmentType: NOT APPLICABLE

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