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Yorodumi- PDB-8pr0: Cytoplasmic dynein-A heavy chain bound to dynactin-p150glued and ... -
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Basic information
| Entry | Database: PDB / ID: 8pr0 | ||||||||||||
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| Title | Cytoplasmic dynein-A heavy chain bound to dynactin-p150glued and IC-LC tower | ||||||||||||
Components |
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Keywords | MOTOR PROTEIN / Dynein / AAA-Atpase / dynactin / p150 / LC8 / TCTEX1 | ||||||||||||
| Function / homology | Function and homology informationintracellular transport of viral protein in host cell / nitric-oxide synthase inhibitor activity / deoxyribonuclease inhibitor activity / negative regulation of DNA strand resection involved in replication fork processing / secretory vesicle / centriolar subdistal appendage / negative regulation of phosphorylation / positive regulation of neuromuscular junction development / centriole-centriole cohesion / intraciliary retrograde transport ...intracellular transport of viral protein in host cell / nitric-oxide synthase inhibitor activity / deoxyribonuclease inhibitor activity / negative regulation of DNA strand resection involved in replication fork processing / secretory vesicle / centriolar subdistal appendage / negative regulation of phosphorylation / positive regulation of neuromuscular junction development / centriole-centriole cohesion / intraciliary retrograde transport / Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / transport along microtubule / Recruitment of mitotic centrosome proteins and complexes / microtubule anchoring at centrosome / dynein light chain binding / ventral spinal cord development / dynein heavy chain binding / Activation of BIM and translocation to mitochondria / motile cilium assembly / retromer complex / ciliary tip / microtubule plus-end / nuclear membrane disassembly / Intraflagellar transport / positive regulation of intracellular transport / positive regulation of microtubule nucleation / negative regulation of nitric oxide biosynthetic process / regulation of metaphase plate congression / positive regulation of spindle assembly / melanosome transport / establishment of spindle localization / regulation of G protein-coupled receptor signaling pathway / microtubule-dependent intracellular transport of viral material towards nucleus / non-motile cilium assembly / dynein complex / retrograde transport, endosome to Golgi / COPI-independent Golgi-to-ER retrograde traffic / retrograde axonal transport / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / P-body assembly / microtubule motor activity / Recruitment of NuMA to mitotic centrosomes / microtubule associated complex / minus-end-directed microtubule motor activity / centrosome localization / COPI-mediated anterograde transport / dynein light intermediate chain binding / cytoplasmic dynein complex / microtubule-based movement / neuromuscular process / nuclear migration / Macroautophagy / neuromuscular junction development / cell leading edge / motor behavior / dynein intermediate chain binding / establishment of mitotic spindle orientation / tertiary granule membrane / ficolin-1-rich granule membrane / spermatid development / enzyme inhibitor activity / positive regulation of insulin secretion involved in cellular response to glucose stimulus / intercellular bridge / COPI-mediated anterograde transport / cytoplasmic microtubule / cytoplasmic microtubule organization / axon cytoplasm / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / neuron projection maintenance / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / centriole / Recruitment of mitotic centrosome proteins and complexes / MHC class II antigen presentation / substantia nigra development / Mitotic Prometaphase / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / EML4 and NUDC in mitotic spindle formation / stress granule assembly / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / AURKA Activation by TPX2 / regulation of mitotic spindle organization / Resolution of Sister Chromatid Cohesion / mitotic spindle organization / filopodium / RHO GTPases Activate Formins / cellular response to nerve growth factor stimulus / neuron cellular homeostasis / negative regulation of neurogenesis / kinetochore / microtubule cytoskeleton organization / spindle / HCMV Early Events / spindle pole Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human)![]() | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 9.4 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. | ||||||||||||
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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 | 8pr0.cif.gz | 571.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8pr0.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8pr0.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pr/8pr0 ftp://data.pdbj.org/pub/pdb/validation_reports/pr/8pr0 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 17830MC ![]() 8pqvC ![]() 8pqwC ![]() 8pqyC ![]() 8pqzC ![]() 8pr1C ![]() 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
-Cytoplasmic dynein 1 ... , 3 types, 5 molecules DCBAK
| #1: 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: ![]() #5: 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: ![]() #6: Protein | | Mass: 54173.156 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNC1LI2, DNCLI2, LIC2 / Production host: ![]() |
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-Dynein light chain ... , 2 types, 4 molecules FEGH
| #2: 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, TCTEL1, TCTEX-1, TCTEX1 / Production host: ![]() |
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-Protein , 1 types, 2 molecules IJ
| #4: Protein | Mass: 142015.484 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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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: all / 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: 9.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 42909 / 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
