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Yorodumi- EMDB-45689: The Outer Dynein Arm-Docking Complex (ODA-DC) from bovine Fallopi... -
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Basic information
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| Title | The Outer Dynein Arm-Docking Complex (ODA-DC) from bovine Fallopian tube | |||||||||
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Keywords | axoneme / cilia / microtubule / dynein / Fallopian tube / doublet microtubule (DMT) / sperm / STRUCTURAL PROTEIN | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.64 Å | |||||||||
Authors | Sun C / Zhang R | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Nature / Year: 2025Title: Structural diversity of axonemes across mammalian motile cilia. Authors: Miguel Ricardo Leung / Chen Sun / Jianwei Zeng / Jacob R Anderson / Qingwei Niu / Wei Huang / Willem E M Noteborn / Alan Brown / Tzviya Zeev-Ben-Mordehai / Rui Zhang / ![]() Abstract: Reproduction, development and homeostasis depend on motile cilia, whose rhythmic beating is powered by a microtubule-based molecular machine called the axoneme. Although an atomic model of the ...Reproduction, development and homeostasis depend on motile cilia, whose rhythmic beating is powered by a microtubule-based molecular machine called the axoneme. Although an atomic model of the axoneme is available for the alga Chlamydomonas reinhardtii, structures of mammalian axonemes are incomplete. Furthermore, we do not fully understand how molecular structures of axonemes vary across motile-ciliated cell types in the body. Here we use cryoelectron microscopy, cryoelectron tomography and proteomics to resolve the 96-nm modular repeat of axonemal doublet microtubules (DMTs) from both sperm flagella and epithelial cilia of the oviduct, brain ventricles and respiratory tract. We find that sperm DMTs are the most specialized, with epithelial cilia having only minor differences across tissues. We build a model of the mammalian sperm DMT, defining the positions and interactions of 181 proteins including 34 newly identified proteins. We elucidate the composition of radial spoke 3 and uncover binding sites of kinases associated with regeneration of ATP and regulation of ciliary motility. We discover a sperm-specific, axoneme-tethered T-complex protein ring complex (TRiC) chaperone that may contribute to construction or maintenance of the long flagella of mammalian sperm. We resolve axonemal dyneins in their prestroke states, illuminating conformational changes that occur during ciliary movement. Our results illustrate how elements of chemical and mechanical regulation are embedded within the axoneme, providing valuable resources for understanding the aetiology of ciliopathy and infertility, and exemplifying the discovery power of modern structural biology. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_45689.map.gz | 255.6 MB | EMDB map data format | |
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| Header (meta data) | emd-45689-v30.xml emd-45689.xml | 15.6 KB 15.6 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_45689_fsc.xml | 16.8 KB | Display | FSC data file |
| Images | emd_45689.png | 375.4 KB | ||
| Masks | emd_45689_msk_1.map | 512 MB | Mask map | |
| Filedesc metadata | emd-45689.cif.gz | 4.2 KB | ||
| Others | emd_45689_additional_1.map.gz emd_45689_half_map_1.map.gz emd_45689_half_map_2.map.gz | 10.8 MB 474.9 MB 474.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-45689 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-45689 | HTTPS FTP |
-Validation report
| Summary document | emd_45689_validation.pdf.gz | 1.3 MB | Display | EMDB validaton report |
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| Full document | emd_45689_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | emd_45689_validation.xml.gz | 26.6 KB | Display | |
| Data in CIF | emd_45689_validation.cif.gz | 35.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-45689 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-45689 | 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_45689.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.34 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_45689_msk_1.map | ||||||||||||
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-Additional map: #1
| File | emd_45689_additional_1.map | ||||||||||||
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-Half map: #1
| File | emd_45689_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_45689_half_map_2.map | ||||||||||||
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Sample components
-Entire : cilia from bovine Fallopian tube
| Entire | Name: cilia from bovine Fallopian tube |
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| Components |
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-Supramolecule #1: cilia from bovine Fallopian tube
| Supramolecule | Name: cilia from bovine Fallopian tube / type: organelle_or_cellular_component / ID: 1 / Parent: 0 |
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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: 7.4 |
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| Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 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: 2.5 µm / Nominal defocus min: 0.5 µm |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Authors
United States, 1 items
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Processing
FIELD EMISSION GUN


