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Open data
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Basic information
| Entry | Database: PDB / ID: 8pr1 | ||||||||||||
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| Title | Cytoplasmic dynein-B heavy chain bound to IC-LC tower | ||||||||||||
Components |
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Keywords | MOTOR PROTEIN / Dynein / AAA-Atpase / LC8 / TCTEX1 | ||||||||||||
| Function / homology | Function and homology informationintracellular transport of viral protein in host cell / negative regulation of DNA strand resection involved in replication fork processing / secretory vesicle / visual behavior / nitric-oxide synthase inhibitor activity / outer dynein arm / dynein light chain binding / transport along microtubule / dynein heavy chain binding / negative regulation of phosphorylation ...intracellular transport of viral protein in host cell / negative regulation of DNA strand resection involved in replication fork processing / secretory vesicle / visual behavior / nitric-oxide synthase inhibitor activity / outer dynein arm / dynein light chain binding / transport along microtubule / dynein heavy chain binding / negative regulation of phosphorylation / Activation of BIM and translocation to mitochondria / motile cilium assembly / dynein complex / Intraflagellar transport / intraciliary retrograde transport / positive regulation of intracellular transport / positive regulation of spindle assembly / regulation of metaphase plate congression / establishment of spindle localization / positive regulation of mitotic cell cycle spindle assembly checkpoint / retrograde axonal transport / male germ cell nucleus / COPI-independent Golgi-to-ER retrograde traffic / microtubule motor activity / spermatid development / minus-end-directed microtubule motor activity / P-body assembly / dynein light intermediate chain binding / cytoplasmic dynein complex / nuclear migration / microtubule-based movement / dynein intermediate chain binding / Macroautophagy / tertiary granule membrane / ficolin-1-rich granule membrane / cytoplasmic microtubule / COPI-mediated anterograde transport / ciliary tip / cytoplasmic microtubule organization / axon cytoplasm / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Recruitment of mitotic centrosome proteins and complexes / MHC class II antigen presentation / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / substantia nigra development / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / regulation of G protein-coupled receptor signaling pathway / AURKA Activation by TPX2 / Resolution of Sister Chromatid Cohesion / mitotic spindle organization / stress granule assembly / enzyme inhibitor activity / regulation of mitotic spindle organization / positive regulation of insulin secretion involved in cellular response to glucose stimulus / filopodium / establishment of mitotic spindle orientation / microtubule cytoskeleton organization / cellular response to nerve growth factor stimulus / RHO GTPases Activate Formins / negative regulation of neurogenesis / mitotic spindle / kinetochore / spindle / HCMV Early Events / Aggrephagy / azurophil granule lumen / Separation of Sister Chromatids / Regulation of PLK1 Activity at G2/M Transition / late endosome / cilium / host cell / microtubule / positive regulation of cold-induced thermogenesis / site of double-strand break / Dengue Virus-Host Interactions / scaffold protein binding / secretory granule lumen / cell cortex / ficolin-1-rich granule lumen / cytoskeleton / vesicle / protein domain specific binding / chromosome / centrosome / Neutrophil degranulation / protein-containing complex binding / Golgi apparatus / enzyme binding / mitochondrion / RNA binding / extracellular exosome / nucleoplasm / ATP binding / extracellular region / membrane Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 8.2 Å | ||||||||||||
Authors | Singh, K. / Lau, C.K. / Manigrasso, G. / Gassmann, R. / Carter, A.P. | ||||||||||||
| Funding support | United Kingdom, European Union, 3items
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Citation | Journal: Science / Year: 2024Title: 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
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8pr1.cif.gz | 652.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8pr1.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8pr1.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pr/8pr1 ftp://data.pdbj.org/pub/pdb/validation_reports/pr/8pr1 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 17831MC ![]() 8pqwC ![]() 8pqyC ![]() 8pqzC ![]() 8pr0C ![]() 8pr2C ![]() 8pr3C ![]() 8pr4C ![]() 8pr5C ![]() 8ptkC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-Dynein light chain ... , 3 types, 6 molecules DEKLts
| #1: Protein | Mass: 10381.899 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNLL1, DLC1, DNCL1, DNCLC1, HDLC1 / Production host: ![]() #3: Protein | Mass: 12461.996 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNLT1 / Production host: ![]() #6: Protein | Mass: 10934.576 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNLRB1, BITH, DNCL2A, DNLC2A, ROBLD1, HSPC162 / Production host: ![]() |
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-Cytoplasmic dynein 1 ... , 3 types, 6 molecules IJAGFH
| #2: Protein | Mass: 68442.141 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNC1I2, DNCI2, DNCIC2 / Production host: ![]() #4: Protein | Mass: 533055.125 Da / Num. of mol.: 2 / Mutation: R1567E, K1610E Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325 / Production host: ![]() #5: Protein | Mass: 54173.156 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNC1LI2, DNCLI2, LIC2 / Production host: ![]() |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Cytoplasmic dynein-A heavy chain bound to dynactin p150 and IC-LC tower Type: COMPLEX / Entity ID: #1-#5 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.2 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 4000 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 53 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
| 3D reconstruction | Resolution: 8.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 42405 / Symmetry type: POINT | ||||||||||||
| Atomic model building | PDB-ID: 7Z8G Accession code: 7Z8G / Source name: PDB / Type: experimental model |
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About Yorodumi




Homo sapiens (human)
United Kingdom, European Union, 3items
Citation




















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FIELD EMISSION GUN
