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Yorodumi- EMDB-17835: Consensus cryo-EM structure of Dynein-Dynactin-JIP3(1-185)-LIS1 -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-17835 | ||||||||||||
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Title | Consensus cryo-EM structure of Dynein-Dynactin-JIP3(1-185)-LIS1 | ||||||||||||
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Sample |
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Keywords | Dynein / AAA-Atpase / p150 / LIS1 / MOTOR PROTEIN / Dynactin / JIP3 | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.5 Å | ||||||||||||
Authors | Singh K / Lau CK / Manigrasso G / Gassmann R / Carter AP | ||||||||||||
Funding support | United Kingdom, European Union, 3 items
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Citation | Journal: Science / Year: 2024 Title: Molecular mechanism of dynein-dynactin complex assembly by LIS1. Authors: Kashish Singh / Clinton K Lau / Giulia Manigrasso / José B Gama / Reto Gassmann / Andrew P Carter / Abstract: Cytoplasmic dynein is a microtubule motor vital for cellular organization and division. It functions as a ~4-megadalton complex containing its cofactor dynactin and a cargo-specific coiled-coil ...Cytoplasmic dynein is a microtubule motor vital for cellular organization and division. It functions as a ~4-megadalton complex containing its cofactor dynactin and a cargo-specific coiled-coil adaptor. However, how dynein and dynactin recognize diverse adaptors, how they interact with each other during complex formation, and the role of critical regulators such as lissencephaly-1 (LIS1) protein (LIS1) remain unclear. In this study, we determined the cryo-electron microscopy structure of dynein-dynactin on microtubules with LIS1 and the lysosomal adaptor JIP3. This structure reveals the molecular basis of interactions occurring during dynein activation. We show how JIP3 activates dynein despite its atypical architecture. Unexpectedly, LIS1 binds dynactin's p150 subunit, tethering it along the length of dynein. Our data suggest that LIS1 and p150 constrain dynein-dynactin to ensure efficient complex formation. | ||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_17835.map.gz | 1.6 GB | EMDB map data format | |
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Header (meta data) | emd-17835-v30.xml emd-17835.xml | 17.9 KB 17.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_17835_fsc.xml | 28.3 KB | Display | FSC data file |
Images | emd_17835.png | 55.2 KB | ||
Masks | emd_17835_msk_1.map | 1.9 GB | Mask map | |
Filedesc metadata | emd-17835.cif.gz | 4.2 KB | ||
Others | emd_17835_additional_1.map.gz emd_17835_half_map_1.map.gz emd_17835_half_map_2.map.gz | 1.8 GB 1.6 GB 1.6 GB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17835 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17835 | HTTPS FTP |
-Validation report
Summary document | emd_17835_validation.pdf.gz | 961.7 KB | Display | EMDB validaton report |
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Full document | emd_17835_full_validation.pdf.gz | 961.2 KB | Display | |
Data in XML | emd_17835_validation.xml.gz | 36.4 KB | Display | |
Data in CIF | emd_17835_validation.cif.gz | 49.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17835 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17835 | HTTPS FTP |
-Related structure data
Related structure data | 8pqvC 8pqwC 8pqyC 8pqzC 8pr0C 8pr1C 8pr2C 8pr3C 8pr4C 8pr5C 8ptkC C: citing same article (ref.) |
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-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_17835.map.gz / Format: CCP4 / Size: 1.9 GB / 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: 1.059 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_17835_msk_1.map | ||||||||||||
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Density Histograms |
-Additional map: Postprocessed map
File | emd_17835_additional_1.map | ||||||||||||
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Annotation | Postprocessed map | ||||||||||||
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Density Histograms |
-Half map: #1
File | emd_17835_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_17835_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Composite structure of Dynein-Dynactin-JIP3-LIS1
Entire | Name: Composite structure of Dynein-Dynactin-JIP3-LIS1 |
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Components |
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-Supramolecule #1: Composite structure of Dynein-Dynactin-JIP3-LIS1
Supramolecule | Name: Composite structure of Dynein-Dynactin-JIP3-LIS1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7, #9, #11, #10, #12, #8, #13-#19 |
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Source (natural) | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.2 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 53.0 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: 4.0 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Initial model | PDB ID: Chain - Source name: PDB / Chain - Initial model type: experimental model |
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Software | Name: UCSF Chimera |