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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Consensus map of dynein-dynactin on microtubules | |||||||||
Map data | Consensus map of dynein-dynactin bound to microtubules | |||||||||
Sample |
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Keywords | dynein / dynactin / microtubule / MOTOR PROTEIN | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 12.0 Å | |||||||||
Authors | Rao Q / Chai P / Zhang K | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Nature / Year: 2026Title: Roles of microtubules and LIS1 in dynein transport machinery assembly. Authors: Qinhui Rao / Jun Yang / Pengxin Chai / Steven Markus / Kai Zhang / ![]() Abstract: Cytoplasmic dynein-1, a microtubule (MT)-based motor protein, requires dynactin and a coiled-coil adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The roles of MTs and dynein ...Cytoplasmic dynein-1, a microtubule (MT)-based motor protein, requires dynactin and a coiled-coil adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The roles of MTs and dynein regulator lissencephaly-1 (LIS1) in DDA assembly have remained elusive. Here we use cryo-electron microscopy to determine the structural basis of MT- and LIS1-mediated DDA assembly. We show that an adaptor-independent dynein-dynactin complex spontaneously forms on MTs with an intrinsic 2:1 stoichiometry in a highly efficient manner, driven by parallel alignment of dynein tails upon MT binding. Adaptors can wedge into and exchange within the assembled MT-bound dynein-dynactin complex; these processes are enabled by relative rotations between dynein and dynactin and facilitated by the dynein light-intermediate chains that assist the adaptor 'search' mechanism. Although LIS1 is dispensable for efficient DD(A)-MT assembly, its presence expands the conformational landscape of DD(A) assemblies on MTs. Cryo-electron microscopy reveals that LIS1 bridges dynactin p150 and dynein in both the closed Phi-like and open prepowerstroke states, stabilizing low-MT-affinity intermediates that tether dynein molecules in proximity to MTs and prime them for subsequent DD(A) assembly through alternative pathways. These findings demonstrate the dynamic adaptability of the dynein transport machinery and the coordinated roles of MTs and LIS1 in DDA assembly. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_47061.map.gz | 245.9 MB | EMDB map data format | |
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| Header (meta data) | emd-47061-v30.xml emd-47061.xml | 15 KB 15 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_47061_fsc.xml | 17.2 KB | Display | FSC data file |
| Images | emd_47061.png | 40.4 KB | ||
| Masks | emd_47061_msk_1.map | 512 MB | Mask map | |
| Filedesc metadata | emd-47061.cif.gz | 4 KB | ||
| Others | emd_47061_half_map_1.map.gz emd_47061_half_map_2.map.gz | 474.4 MB 474.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-47061 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-47061 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9dgpC ![]() 9dgqC ![]() 9dgrC ![]() 9dgsC ![]() 9dgtC ![]() 9dguC ![]() 9dgvC ![]() 9yncC ![]() 9yndC ![]() 9yneC ![]() 9ynfC ![]() 9yngC ![]() 9ynhC C: citing same article ( |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_47061.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Consensus map of dynein-dynactin bound to microtubules | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.65 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_47061_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: half
| File | emd_47061_half_map_1.map | ||||||||||||
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| Annotation | half | ||||||||||||
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| Density Histograms |
-Half map: half
| File | emd_47061_half_map_2.map | ||||||||||||
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| Annotation | half | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : dynein-dynactin on microtubules
| Entire | Name: dynein-dynactin on microtubules |
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| Components |
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-Supramolecule #1: dynein-dynactin on microtubules
| Supramolecule | Name: dynein-dynactin on microtubules / type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 5 MDa |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.2 |
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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: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Calibrated defocus max: 3.0 µm / Calibrated defocus min: 1.2 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
United States, 1 items
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Processing
FIELD EMISSION GUN

