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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 | ||||||||||||
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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 / nitric-oxide synthase inhibitor activity / secretory vesicle / deoxyribonuclease inhibitor activity / negative regulation of DNA strand resection involved in replication fork processing / negative regulation of phosphorylation / transport along microtubule / intraciliary retrograde transport / visual behavior / dynein light chain binding ...intracellular transport of viral protein in host cell / nitric-oxide synthase inhibitor activity / secretory vesicle / deoxyribonuclease inhibitor activity / negative regulation of DNA strand resection involved in replication fork processing / negative regulation of phosphorylation / transport along microtubule / intraciliary retrograde transport / visual behavior / dynein light chain binding / dynein heavy chain binding / Activation of BIM and translocation to mitochondria / motile cilium assembly / ciliary tip / Intraflagellar transport / positive regulation of intracellular transport / negative regulation of nitric oxide biosynthetic process / regulation of metaphase plate congression / positive regulation of spindle assembly / establishment of spindle localization / regulation of G protein-coupled receptor signaling pathway / microtubule-dependent intracellular transport of viral material towards nucleus / dynein complex / COPI-independent Golgi-to-ER retrograde traffic / retrograde axonal transport / P-body assembly / microtubule motor activity / minus-end-directed microtubule motor activity / cytoplasmic dynein complex / dynein light intermediate chain binding / centrosome localization / microtubule-based movement / nuclear migration / Macroautophagy / dynein intermediate chain binding / establishment of mitotic spindle orientation / tertiary granule membrane / ficolin-1-rich granule membrane / enzyme inhibitor activity / spermatid development / positive regulation of insulin secretion involved in cellular response to glucose stimulus / COPI-mediated anterograde transport / cytoplasmic microtubule / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / cytoplasmic microtubule organization / Mitotic Prometaphase / axon cytoplasm / EML4 and NUDC in mitotic spindle formation / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / stress granule assembly / substantia nigra development / 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 / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Resolution of Sister Chromatid Cohesion / regulation of mitotic spindle organization / AURKA Activation by TPX2 / mitotic spindle organization / filopodium / RHO GTPases Activate Formins / cellular response to nerve growth factor stimulus / kinetochore / negative regulation of neurogenesis / microtubule cytoskeleton organization / spindle / HCMV Early Events / Aggrephagy / mitotic spindle / Separation of Sister Chromatids / azurophil granule lumen / Regulation of PLK1 Activity at G2/M Transition / late endosome / nervous system development / host cell / site of double-strand break / positive regulation of cold-induced thermogenesis / scaffold protein binding / cell cortex / secretory granule lumen / vesicle / ficolin-1-rich granule lumen / microtubule / cytoskeleton / cilium / cell division / apoptotic process / DNA damage response / centrosome / Neutrophil degranulation / symbiont entry into host cell / protein-containing complex binding / enzyme binding / Golgi apparatus / ATP hydrolysis activity / mitochondrion / RNA binding / extracellular exosome 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
| Summary document | 8pr1_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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| Full document | 8pr1_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | 8pr1_validation.xml.gz | 76.4 KB | Display | |
| Data in CIF | 8pr1_validation.cif.gz | 132.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pr/8pr1 ftp://data.pdbj.org/pub/pdb/validation_reports/pr/8pr1 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 17831MC ![]() 8pqvC ![]() 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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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
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FIELD EMISSION GUN
