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Open data
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Basic information
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Title | Consensus map of dynein-dynactin-BICDR on microtubules | ||||||||||||
![]() | Consensus map of Dynein-Dynactin-BICDR on microtubules | ||||||||||||
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Biological species | ![]() ![]() ![]() ![]() ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.33 Å | ||||||||||||
![]() | Chaaban S / Carter AP | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of dynein-dynactin on microtubules shows tandem adaptor binding. Authors: Sami Chaaban / Andrew P Carter / ![]() Abstract: Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor. Up to two dynein dimers can be recruited per dynactin, and interactions between ...Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor. Up to two dynein dimers can be recruited per dynactin, and interactions between them affect their combined motile behaviour. Different coiled-coil adaptors are linked to different cargos, and some share motifs known to contact sites on dynein and dynactin. There is limited structural information on how the resulting complex interacts with microtubules and how adaptors are recruited. Here we develop a cryo-electron microscopy processing pipeline to solve the high-resolution structure of dynein-dynactin and the adaptor BICDR1 bound to microtubules. This reveals the asymmetric interactions between neighbouring dynein motor domains and how they relate to motile behaviour. We found that two adaptors occupy the complex. Both adaptors make similar interactions with the dyneins but diverge in their contacts with each other and dynactin. Our structure has implications for the stability and stoichiometry of motor recruitment by cargos. | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 202.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 23.6 KB 23.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 17.2 KB | Display | ![]() |
Images | ![]() | 75 KB | ||
Masks | ![]() | 216 MB | ![]() | |
Others | ![]() ![]() | 193.9 MB 193.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 630.4 KB | Display | ![]() |
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Full document | ![]() | 629.9 KB | Display | |
Data in XML | ![]() | 22.1 KB | Display | |
Data in CIF | ![]() | 29.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | Consensus map of Dynein-Dynactin-BICDR on microtubules | ||||||||||||||||||||
Voxel size | X=Y=Z: 2.489 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: Half map 1 of Dynein-Dynactin-BICDR on microtubules
File | emd_15396_half_map_1.map | ||||||||||||
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Annotation | Half map 1 of Dynein-Dynactin-BICDR on microtubules | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map 2 of Dynein-Dynactin-BICDR on microtubules
File | emd_15396_half_map_2.map | ||||||||||||
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Annotation | Half map 2 of Dynein-Dynactin-BICDR on microtubules | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Complex of dynein, dynactin, and BICDR1 bound to microtubules
Entire | Name: Complex of dynein, dynactin, and BICDR1 bound to microtubules |
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Components |
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-Supramolecule #1: Complex of dynein, dynactin, and BICDR1 bound to microtubules
Supramolecule | Name: Complex of dynein, dynactin, and BICDR1 bound to microtubules type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: #1-#7 |
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Molecular weight | Theoretical: 4 MDa |
-Supramolecule #2: Dynein, cytoplasmic 1
Supramolecule | Name: Dynein, cytoplasmic 1 / type: organelle_or_cellular_component / ID: 2 / Parent: 1 / Macromolecule list: #13-#16 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 1.4 MDa |
Recombinant expression | Organism: ![]() ![]() |
-Supramolecule #3: Dynactin
Supramolecule | Name: Dynactin / type: organelle_or_cellular_component / ID: 3 / Parent: 1 / Macromolecule list: #1-#10 |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 1.1 MDa |
-Supramolecule #4: BICDR1
Supramolecule | Name: BICDR1 / type: organelle_or_cellular_component / ID: 4 / Parent: 1 / Macromolecule list: #11 |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 130 KDa |
Recombinant expression | Organism: ![]() ![]() |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.2 Component:
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293.15 K / Instrument: FEI VITROBOT MARK IV / Details: 20 second incubation. |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 14 / Number real images: 88715 / Average exposure time: 3.0 sec. / Average electron dose: 53.0 e/Å2 Details: Images were collected in movie-mode and fractionated into 53 movie frames |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 4.0 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 81000 |
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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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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