+
Open data
-
Basic information
| Entry | ![]() | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | Composite map of proximal A-C linker of Tetrahymena centriole | ||||||||||||
Map data | Composite map of Tetrahymena proximal A-C linker | ||||||||||||
Sample |
| ||||||||||||
Keywords | centriole / basal body / centrosome / STRUCTURAL PROTEIN | ||||||||||||
| Function / homology | Function and homology informationMWP complex / cell projection organization / centrosome cycle / microtubule organizing center / cilium assembly / centriole / centriolar satellite / ciliary basal body / centrosome / cytoplasm Similarity search - Function | ||||||||||||
| 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
| ||||||||||||
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 |
|
-
Structure visualization
| Supplemental images |
|---|
-
Downloads & links
-EMDB archive
| Map data | emd_53467.map.gz | 31.2 MB | EMDB map data format | |
|---|---|---|---|---|
| Header (meta data) | emd-53467-v30.xml emd-53467.xml | 37.3 KB 37.3 KB | Display Display | EMDB header |
| Images | emd_53467.png | 77.3 KB | ||
| Filedesc metadata | emd-53467.cif.gz | 8.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-53467 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-53467 | HTTPS FTP |
-Validation report
| Summary document | emd_53467_validation.pdf.gz | 516.3 KB | Display | EMDB validaton report |
|---|---|---|---|---|
| Full document | emd_53467_full_validation.pdf.gz | 515.9 KB | Display | |
| Data in XML | emd_53467_validation.xml.gz | 8 KB | Display | |
| Data in CIF | emd_53467_validation.cif.gz | 9.3 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-53467 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-53467 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9qzcMC ![]() 9qzfC C: citing same article ( M: atomic model generated by this map |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
|---|
-
Map
| File | Download / File: emd_53467.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Annotation | Composite map of Tetrahymena proximal A-C linker | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.315 Å | ||||||||||||||||||||||||||||||||||||
| Density |
| ||||||||||||||||||||||||||||||||||||
| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
|
-Supplemental data
-
Sample components
+Entire : proximal A-C linker of Tetrahymena thermophila basal body centriole
+Supramolecule #1: proximal A-C linker of Tetrahymena thermophila basal body centriole
+Macromolecule #1: WD repeat WRAP73-like protein, putative
+Macromolecule #2: Centrosomal protein, putative
+Macromolecule #3: Rab-GAP TBC domain-containing protein
+Macromolecule #4: TBC1 domain family member 31
+Macromolecule #5: POC1 centriolar protein homolog
+Macromolecule #6: Unknown Protein Chain
+Macromolecule #7: Unknown Protein Chain
+Macromolecule #8: SWIM-type domain-containing protein
+Macromolecule #9: Unknown Protein Chain
+Macromolecule #10: Unknown Protein Chain
+Macromolecule #11: Unknown Protein Chain
+Macromolecule #12: Unknown Protein Chain
+Macromolecule #13: Unknown Protein Chain
+Macromolecule #14: Unknown Protein Chain
+Macromolecule #15: Unknown Protein Chain
-Experimental details
-Structure determination
| Method | cryo EM |
|---|---|
Processing | single particle reconstruction |
| Aggregation state | filament |
-
Sample preparation
| Buffer | pH: 7.5 |
|---|---|
| Vitrification | Cryogen name: ETHANE-PROPANE |
-
Electron microscopy
| Microscope | TFS KRIOS |
|---|---|
| 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 |
Movie
Controller
About Yorodumi




Keywords
Authors
Switzerland, 3 items
Citation






















Z (Sec.)
Y (Row.)
X (Col.)




















Processing
FIELD EMISSION GUN
