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Yorodumi- EMDB-42781: Triplet microtubule from the proximal region of basal body, focus... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-42781 | |||||||||
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Title | Triplet microtubule from the proximal region of basal body, focusing on the B/C inner junction, wildtype Tetrahymena themorphila | |||||||||
Map data | triplet microtubule from the proximal region of basal body, focusing on the B/C inner junction, wildtype Tetrahymena thermophila | |||||||||
Sample |
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Keywords | cilia / basal body / microtubule / CYTOSOLIC PROTEIN | |||||||||
Biological species | Tetrahymena thermophila (eukaryote) | |||||||||
Method | subtomogram averaging / cryo EM / Resolution: 10.0 Å | |||||||||
Authors | Ruehle M / Li S / Agard DA / Pearson C | |||||||||
Funding support | United States, 2 items
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Citation | Journal: J Cell Biol / Year: 2024 Title: Poc1 bridges basal body inner junctions to promote triplet microtubule integrity and connections. Authors: Marisa D Ruehle / Sam Li / David A Agard / Chad G Pearson / Abstract: Basal bodies (BBs) are conserved eukaryotic structures that organize cilia. They are comprised of nine, cylindrically arranged, triplet microtubules (TMTs) connected to each other by inter-TMT ...Basal bodies (BBs) are conserved eukaryotic structures that organize cilia. They are comprised of nine, cylindrically arranged, triplet microtubules (TMTs) connected to each other by inter-TMT linkages which stabilize the structure. Poc1 is a conserved protein important for BB structural integrity in the face of ciliary forces transmitted to BBs. To understand how Poc1 confers BB stability, we identified the precise position of Poc1 in the Tetrahymena BB and the effect of Poc1 loss on BB structure. Poc1 binds at the TMT inner junctions, stabilizing TMTs directly. From this location, Poc1 also stabilizes inter-TMT linkages throughout the BB, including the cartwheel pinhead and the inner scaffold. The full localization of the inner scaffold protein Fam161A requires Poc1. As ciliary forces are increased, Fam161A is reduced, indicative of a force-dependent molecular remodeling of the inner scaffold. Thus, while not essential for BB assembly, Poc1 promotes BB interconnections that establish an architecture competent to resist ciliary forces. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_42781.map.gz | 14.7 MB | EMDB map data format | |
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Header (meta data) | emd-42781-v30.xml emd-42781.xml | 14.9 KB 14.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_42781_fsc.xml | 5.8 KB | Display | FSC data file |
Images | emd_42781.png | 50.5 KB | ||
Masks | emd_42781_msk_1.map | 15.6 MB | Mask map | |
Filedesc metadata | emd-42781.cif.gz | 4.3 KB | ||
Others | emd_42781_half_map_1.map.gz emd_42781_half_map_2.map.gz | 7.7 MB 7.7 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-42781 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-42781 | HTTPS FTP |
-Validation report
Summary document | emd_42781_validation.pdf.gz | 1011.7 KB | Display | EMDB validaton report |
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Full document | emd_42781_full_validation.pdf.gz | 1011.3 KB | Display | |
Data in XML | emd_42781_validation.xml.gz | 11.4 KB | Display | |
Data in CIF | emd_42781_validation.cif.gz | 15.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-42781 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-42781 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_42781.map.gz / Format: CCP4 / Size: 15.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | triplet microtubule from the proximal region of basal body, focusing on the B/C inner junction, wildtype Tetrahymena thermophila | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 2.7 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_42781_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_42781_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_42781_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Triplet microtubule from basal body isolated from Tetrahymena the...
Entire | Name: Triplet microtubule from basal body isolated from Tetrahymena thermophila |
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Components |
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-Supramolecule #1: Triplet microtubule from basal body isolated from Tetrahymena the...
Supramolecule | Name: Triplet microtubule from basal body isolated from Tetrahymena thermophila type: organelle_or_cellular_component / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Tetrahymena thermophila (eukaryote) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | subtomogram averaging |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 / Details: 1xTE |
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Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK III |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Temperature | Min: 78.0 K / Max: 78.0 K |
Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 6000 pixel / Digitization - Dimensions - Height: 4000 pixel / Number real images: 2 / Average exposure time: 0.36 sec. / Average electron dose: 1.33 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 2.0 µm / Nominal magnification: 33000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |