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- EMDB-7481: The tether and tether head complex and I1 dynein complex region e... -

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Basic information

Entry
Database: EMDB / ID: EMD-7481
TitleThe tether and tether head complex and I1 dynein complex region extracted from the cryo-electron tomography and subtomographic average (3736 axonemal repeats) of isolated Chlamydomonas wild type cilia
Map dataCryo-electron tomography and subtomographic average (3736 axonemal repeats) of isolated axonemes from Chlamydomonas wide type
Sample
  • Organelle or cellular component: The tether and tether head complex and I1 dynein complex extracted from the cryo-electron tomography and subtomographic average (3736 axonemal repeats) of isolated Chlamydomonas wild type cilia
Biological speciesChlamydomonas reinhardtii (plant)
Methodsubtomogram averaging / cryo EM / Resolution: 30.0 Å
AuthorsFu G / Wang Q / Phan N / Urbanska P / Joachimiak E / Lin J / Wloga D / Nicastro D
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research InstituteR01GM083122 United States
CitationJournal: Mol Biol Cell / Year: 2018
Title: The I1 dynein-associated tether and tether head complex is a conserved regulator of ciliary motility.
Authors: Gang Fu / Qian Wang / Nhan Phan / Paulina Urbanska / Ewa Joachimiak / Jianfeng Lin / Dorota Wloga / Daniela Nicastro /
Abstract: Motile cilia are essential for propelling cells and moving fluids across tissues. The activity of axonemal dynein motors must be precisely coordinated to generate ciliary motility, but their ...Motile cilia are essential for propelling cells and moving fluids across tissues. The activity of axonemal dynein motors must be precisely coordinated to generate ciliary motility, but their regulatory mechanisms are not well understood. The tether and tether head (T/TH) complex was hypothesized to provide mechanical feedback during ciliary beating because it links the motor domains of the regulatory I1 dynein to the ciliary doublet microtubule. Combining genetic and biochemical approaches with cryoelectron tomography, we identified FAP44 and FAP43 (plus the algae-specific, FAP43-redundant FAP244) as T/TH components. WT-mutant comparisons revealed that the heterodimeric T/TH complex is required for the positional stability of the I1 dynein motor domains, stable anchoring of CK1 kinase, and proper phosphorylation of the regulatory IC138-subunit. T/TH also interacts with inner dynein arm d and radial spoke 3, another important motility regulator. The T/TH complex is a conserved regulator of I1 dynein and plays an important role in the signaling pathway that is critical for normal ciliary motility.
History
DepositionFeb 26, 2018-
Header (metadata) releaseMar 14, 2018-
Map releaseJan 9, 2019-
UpdateJul 24, 2019-
Current statusJul 24, 2019Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 131
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 131
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_7481.png

Downloads & links

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Map

FileDownload / File: emd_7481.map.gz / Format: CCP4 / Size: 516.6 KB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCryo-electron tomography and subtomographic average (3736 axonemal repeats) of isolated axonemes from Chlamydomonas wide type
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
9.86 Å/pix.
x 55 pix.
= 542.08 Å		9.86 Å/pix.
x 40 pix.
= 394.24 Å		9.86 Å/pix.
x 60 pix.
= 591.36 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

generated in cubic-lattice coordinate

Voxel sizeX=Y=Z: 9.856 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy EMDB: 131.0 / Movie #1: 131
Minimum - Maximum94.501434000000003 - 176.396420000000006
Average (Standard dev.)126.001075999999998 (±10.275537)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-30-39-31
Dimensions406055
Spacing604055
CellA: 591.36005 Å / B: 394.24005 Å / C: 542.0801 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z9.8569.8569.856
M x/y/z604055
origin x/y/z0.0000.0000.000
length x/y/z591.360394.240542.080
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS-39-30-31
NC/NR/NS604055
D min/max/mean94.501176.396126.001

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Supplemental data

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Sample components

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Entire : The tether and tether head complex and I1 dynein complex extracte...

EntireName: The tether and tether head complex and I1 dynein complex extracted from the cryo-electron tomography and subtomographic average (3736 axonemal repeats) of isolated Chlamydomonas wild type cilia
Components
  • Organelle or cellular component: The tether and tether head complex and I1 dynein complex extracted from the cryo-electron tomography and subtomographic average (3736 axonemal repeats) of isolated Chlamydomonas wild type cilia

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Supramolecule #1: The tether and tether head complex and I1 dynein complex extracte...

SupramoleculeName: The tether and tether head complex and I1 dynein complex extracted from the cryo-electron tomography and subtomographic average (3736 axonemal repeats) of isolated Chlamydomonas wild type cilia
type: organelle_or_cellular_component / ID: 1 / Parent: 0
Source (natural)Organism: Chlamydomonas reinhardtii (plant) / Strain: wild type

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Experimental details

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Structure determination

Methodcryo EM
Processingsubtomogram averaging
Aggregation statetissue

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Sample preparation

BufferpH: 7.4
Component:
ConcentrationFormulaName
30.0 mMC8H18N2O4SHEPES
25.0 mMKClpotassium chloride
5.0 mMMgSO4magnesium sulfate
1.0 mMEGTA
0.1 mMEDTA

Details: Solutions were freshly made before use.
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 101.325 kPa
VitrificationCryogen name: ETHANE / Chamber temperature: 100 K / Instrument: HOMEMADE PLUNGER
Details: back-side blotting for 1.5-2.5 seconds before plunging.

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Electron microscopy

MicroscopeFEI TECNAI F30
Specialist opticsEnergy filter - Name: GIF 2000 / Energy filter - Lower energy threshold: 0 eV / Energy filter - Upper energy threshold: 20 eV
Image recordingFilm or detector model: GATAN ULTRASCAN 1000 (2k x 2k) / Average electron dose: 1.5 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 / Nominal magnification: 13500
Sample stageSpecimen holder model: GATAN LIQUID NITROGEN / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Tecnai F30 / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 30.0 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: IMOD
Software - details: fiducial alignment and weighted backprojection
Number subtomograms used: 3736
ExtractionNumber tomograms: 25 / Number images used: 3736 / Software - Name: MATLAB
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: PEET

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