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Yorodumi- EMDB-41376: 96nm repeat of Doublet microtubule from Tetrahymena thermophila -
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Open data
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Basic information
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| Title | 96nm repeat of Doublet microtubule from Tetrahymena thermophila | |||||||||
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Sample |
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Keywords | nexin-dynein regulatory complex / cilia / axoneme dynein / STRUCTURAL PROTEIN | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 5.54 Å | |||||||||
Authors | Ghanaeian AG / Bui KH | |||||||||
| Funding support | Canada, 2 items
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Citation | Journal: Nat Commun / Year: 2023Title: Integrated modeling of the Nexin-dynein regulatory complex reveals its regulatory mechanism. Authors: Avrin Ghanaeian / Sumita Majhi / Caitlyn L McCafferty / Babak Nami / Corbin S Black / Shun Kai Yang / Thibault Legal / Ophelia Papoulas / Martyna Janowska / Melissa Valente-Paterno / Edward ...Authors: Avrin Ghanaeian / Sumita Majhi / Caitlyn L McCafferty / Babak Nami / Corbin S Black / Shun Kai Yang / Thibault Legal / Ophelia Papoulas / Martyna Janowska / Melissa Valente-Paterno / Edward M Marcotte / Dorota Wloga / Khanh Huy Bui / ![]() Abstract: Cilia are hairlike protrusions that project from the surface of eukaryotic cells and play key roles in cell signaling and motility. Ciliary motility is regulated by the conserved nexin-dynein ...Cilia are hairlike protrusions that project from the surface of eukaryotic cells and play key roles in cell signaling and motility. Ciliary motility is regulated by the conserved nexin-dynein regulatory complex (N-DRC), which links adjacent doublet microtubules and regulates and coordinates the activity of outer doublet complexes. Despite its critical role in cilia motility, the assembly and molecular basis of the regulatory mechanism are poorly understood. Here, using cryo-electron microscopy in conjunction with biochemical cross-linking and integrative modeling, we localize 12 DRC subunits in the N-DRC structure of Tetrahymena thermophila. We also find that the CCDC96/113 complex is in close contact with the DRC9/10 in the linker region. In addition, we reveal that the N-DRC is associated with a network of coiled-coil proteins that most likely mediates N-DRC regulatory activity. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_41376.map.gz | 372.7 MB | EMDB map data format | |
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| Header (meta data) | emd-41376-v30.xml emd-41376.xml | 12.3 KB 12.3 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_41376_fsc.xml | 15.4 KB | Display | FSC data file |
| Images | emd_41376.png | 77.9 KB | ||
| Masks | emd_41376_msk_1.map | 396.1 MB | Mask map | |
| Filedesc metadata | emd-41376.cif.gz | 3.8 KB | ||
| Others | emd_41376_half_map_1.map.gz emd_41376_half_map_2.map.gz | 367.4 MB 367.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-41376 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-41376 | HTTPS FTP |
-Validation report
| Summary document | emd_41376_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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| Full document | emd_41376_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | emd_41376_validation.xml.gz | 24.5 KB | Display | |
| Data in CIF | emd_41376_validation.cif.gz | 32.8 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-41376 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-41376 | 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_41376.map.gz / Format: CCP4 / Size: 396.1 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: 2.74 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_41376_msk_1.map | ||||||||||||
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-Half map: #1
| File | emd_41376_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_41376_half_map_2.map | ||||||||||||
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Sample components
-Entire : 96nm repeat of Doublet microtubule from Tetrahymena thermophila
| Entire | Name: 96nm repeat of Doublet microtubule from Tetrahymena thermophila |
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| Components |
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-Supramolecule #1: 96nm repeat of Doublet microtubule from Tetrahymena thermophila
| Supramolecule | Name: 96nm repeat of Doublet microtubule from Tetrahymena thermophila 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 | cell |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 45.0 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: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
Canada, 2 items
Citation










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Processing
FIELD EMISSION GUN


