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- EMDB-10455: Campylobacter jejuni fliH deletion, fliI knockout flagellar motor -

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Basic information

Entry
Database: EMDB / ID: EMD-10455
TitleCampylobacter jejuni fliH deletion, fliI knockout flagellar motor
Map dataC17 processed Flagellar motor of C.jejuni dFliH, FliI::cat-rpsL
Sample
  • Organelle or cellular component: Flagellar motor of Campylobacter jejuni in situ, fliH deletion strain.
Biological speciesCampylobacter jejuni (Campylobacter)
Methodsubtomogram averaging / cryo EM / Resolution: 62.0 Å
AuthorsMatthews-Palmer T / Beeby M
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
The Francis Crick InstituteFC001179 United Kingdom
Medical Research Council (United Kingdom)MR/P019374/1 United Kingdom
CitationJournal: mBio / Year: 2020
Title: Diversification of Campylobacter jejuni Flagellar C-Ring Composition Impacts Its Structure and Function in Motility, Flagellar Assembly, and Cellular Processes.
Authors: Louie D Henderson / Teige R S Matthews-Palmer / Connor J Gulbronson / Deborah A Ribardo / Morgan Beeby / David R Hendrixson /
Abstract: Bacterial flagella are reversible rotary motors that rotate external filaments for bacterial propulsion. Some flagellar motors have diversified by recruiting additional components that influence ...Bacterial flagella are reversible rotary motors that rotate external filaments for bacterial propulsion. Some flagellar motors have diversified by recruiting additional components that influence torque and rotation, but little is known about the possible diversification and evolution of core motor components. The mechanistic core of flagella is the cytoplasmic C ring, which functions as a rotor, directional switch, and assembly platform for the flagellar type III secretion system (fT3SS) ATPase. The C ring is composed of a ring of FliG proteins and a helical ring of surface presentation of antigen (SPOA) domains from the switch proteins FliM and one of two usually mutually exclusive paralogs, FliN or FliY. We investigated the composition, architecture, and function of the C ring of , which encodes FliG, FliM, and both FliY and FliN by a variety of interrogative approaches. We discovered a diversified C ring containing FliG, FliM, and both FliY, which functions as a classical FliN-like protein for flagellar assembly, and FliN, which has neofunctionalized into a structural role. Specific protein interactions drive the formation of a more complex heterooligomeric C-ring structure. We discovered that this complex C ring has additional cellular functions in polarly localizing FlhG for numerical regulation of flagellar biogenesis and spatial regulation of division. Furthermore, mutation of the C ring revealed a T3SS that was less dependent on its ATPase complex for assembly than were other systems. Our results highlight considerable evolved flagellar diversity that impacts motor output, biogenesis, and cellular processes in different species. The conserved core of bacterial flagellar motors reflects a shared evolutionary history that preserves the mechanisms essential for flagellar assembly, rotation, and directional switching. In this work, we describe an expanded and diversified set of core components in the flagellar C ring, the mechanistic core of the motor. Our work provides insight into how usually conserved core components may have diversified by gene duplication, enabling a division of labor of the ancestral protein between the two new proteins, acquisition of new roles in flagellar assembly and motility, and expansion of the function of the flagellum beyond motility, including spatial regulation of cell division and numerical control of flagellar biogenesis in Our results highlight that relatively small changes, such as gene duplications, can have substantial ramifications on the cellular roles of a molecular machine.
History
DepositionNov 5, 2019-
Header (metadata) releaseJan 22, 2020-
Map releaseJan 22, 2020-
UpdateJan 22, 2020-
Current statusJan 22, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Solid view (volume rendering)
  • Imaged by UCSF Chimera
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  • Solid view (volume rendering)
  • Imaged by UCSF Chimera
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Supplemental images

emd_10455.png

Downloads & links

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Map

FileDownload / File: emd_10455.map.gz / Format: CCP4 / Size: 12.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationC17 processed Flagellar motor of C.jejuni dFliH, FliI::cat-rpsL
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
8.28 Å/pix.
x 150 pix.
= 1242. Å		8.28 Å/pix.
x 150 pix.
= 1242. Å		8.28 Å/pix.
x 150 pix.
= 1242. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 8.28 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-1.0570208 - 0.90538
Average (Standard dev.)-0.031115618 (±0.20404054)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions150150150
Spacing150150150
CellA=B=C: 1242.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z8.288.288.28
M x/y/z150150150
origin x/y/z0.0000.0000.000
length x/y/z1242.0001242.0001242.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS150150150
D min/max/mean-1.0570.905-0.031

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Supplemental data

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Sample components

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Entire : Flagellar motor of Campylobacter jejuni in situ, fliH deletion strain.

EntireName: Flagellar motor of Campylobacter jejuni in situ, fliH deletion strain.
Components
  • Organelle or cellular component: Flagellar motor of Campylobacter jejuni in situ, fliH deletion strain.

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Supramolecule #1: Flagellar motor of Campylobacter jejuni in situ, fliH deletion strain.

SupramoleculeName: Flagellar motor of Campylobacter jejuni in situ, fliH deletion strain.
type: organelle_or_cellular_component / ID: 1 / Parent: 0
Source (natural)Organism: Campylobacter jejuni (Campylobacter) / Strain: 81-176 / Organelle: Flagellar motor / Location in cell: cell pole

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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: 7.3
VitrificationCryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 20 K / Instrument: FEI VITROBOT MARK IV
DetailsBacterial cell suspension mixed with 10nm gold fiducial nanoparticles.

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Electron microscopy

MicroscopeFEI TECNAI F20
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 120.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus min: 3.0 µm / Nominal magnification: 25000
Sample stageSpecimen holder model: GATAN 914 HIGH TILT LIQUID NITROGEN CRYO TRANSFER TOMOGRAPHY HOLDER
Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Tecnai F20 / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: C17 (17 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 62.0 Å / Resolution method: FSC 0.5 CUT-OFF
Details: Non-independent half-map FSC of unsymmetrised map used with 0.5 threshold cited as resolution.
Number subtomograms used: 186
ExtractionNumber tomograms: 165 / Number images used: 186 / Method: manual selection / Software - Name: IMOD
Details: reference-free alignment from manual initial co-ordinates & orientations.
Final angle assignmentType: NOT APPLICABLE / Software - Name: PEET

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