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Yorodumi- EMDB-53984: A-link and A-microtubule of Tetrahymena transitional A-C linker -
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Open data
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Basic information
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| Title | A-link and A-microtubule of Tetrahymena transitional A-C linker | ||||||||||||
Map data | A-link and A-microtubule of Tetrahymena transitional A-C linker, B-factor sharpened using relion_postprocess, original pixel size 1.34 | ||||||||||||
Sample |
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Keywords | centriole / basal body / centrosome / STRUCTURAL PROTEIN | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.8 Å | ||||||||||||
Authors | Cai B / Xu JW / Luo L / Aarts E / Leitner A / Ishikawa T / Beltro P / Pilhofer M / Wieczorek M | ||||||||||||
| Funding support | Switzerland, 3 items
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Citation | Journal: Sci Adv / Year: 2025Title: Structure and assembly of the A-C linker connecting microtubule triplets in centrioles. Authors: Bin Cai / Jingwei Xu / Erik H Collet / Ellen Aarts / Leo Luo / Alexander Leitner / Takashi Ishikawa / Pedro Beltrao / Chad G Pearson / Martin Pilhofer / Michal Wieczorek / ![]() Abstract: Centriole assembly involves the coordination of centriolar modules. One module is the A-C linker, an enigmatic protein assembly connecting the A-microtubule of one microtubule triplet to the C- ...Centriole assembly involves the coordination of centriolar modules. One module is the A-C linker, an enigmatic protein assembly connecting the A-microtubule of one microtubule triplet to the C-microtubule of the neighboring triplet. Here, we integrated biochemistry, multiscale cryo-electron microscopy, and AlphaFold modeling to investigate the architecture of the centriole. Using an improved centriole isolation method, we determined the structure of the A-C linker bound to microtubule triplets, which revealed how the A-C linker cross-links microtubules and integrates with the B-C junction. We found marked changes in the structure and composition of the A-C linker that correlate with the presence of other centriolar modules, including the pinhead, cartwheel, and inner scaffold. Our findings show that the A-C linker is a highly integrated component of the centriole whose polymorphism may orchestrate the assembly of spatially distinct centriolar modules, and provide a framework for dissecting the biology of centrioles. | ||||||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_53984.map.gz | 8.7 MB | EMDB map data format | |
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| Header (meta data) | emd-53984-v30.xml emd-53984.xml | 22.9 KB 22.9 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_53984_fsc.xml | 8.6 KB | Display | FSC data file |
| Images | emd_53984.png | 61.5 KB | ||
| Filedesc metadata | emd-53984.cif.gz | 4.6 KB | ||
| Others | emd_53984_additional_1.map.gz emd_53984_additional_2.map.gz emd_53984_half_map_1.map.gz emd_53984_half_map_2.map.gz | 8.7 MB 28.2 MB 41.2 MB 41.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-53984 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-53984 | HTTPS FTP |
-Validation report
| Summary document | emd_53984_validation.pdf.gz | 918.7 KB | Display | EMDB validaton report |
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| Full document | emd_53984_full_validation.pdf.gz | 918.2 KB | Display | |
| Data in XML | emd_53984_validation.xml.gz | 15.5 KB | Display | |
| Data in CIF | emd_53984_validation.cif.gz | 20.5 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-53984 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-53984 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_53984.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | A-link and A-microtubule of Tetrahymena transitional A-C linker, B-factor sharpened using relion_postprocess, original pixel size 1.34 | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.34 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: A-link and A-microtubule of Tetrahymena transitional A-C linker,...
| File | emd_53984_additional_1.map | ||||||||||||
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| Annotation | A-link and A-microtubule of Tetrahymena transitional A-C linker, B-factor sharpened using relion_postprocess, pixel size corrected to 1.315 | ||||||||||||
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| Density Histograms |
-Additional map: A-link and A-microtubule of Tetrahymena transitional A-C linker,...
| File | emd_53984_additional_2.map | ||||||||||||
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| Annotation | A-link and A-microtubule of Tetrahymena transitional A-C linker, processed with EMReady, pixel size corrected to 1.315 | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_53984_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_53984_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Transitional A-C linker of Tetrahymena thermophila basal body cen...
| Entire | Name: Transitional A-C linker of Tetrahymena thermophila basal body centriole |
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| Components |
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-Supramolecule #1: Transitional A-C linker of Tetrahymena thermophila basal body cen...
| Supramolecule | Name: Transitional A-C linker of Tetrahymena thermophila basal body centriole type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: #1-#27 |
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| Source (natural) | Organism: ![]() |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 35.0 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: 3.0 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
Switzerland, 3 items
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Processing
FIELD EMISSION GUN

