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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 information Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / intracellular transport of viral protein in host cell / secretory vesicle / positive regulation of neuromuscular junction development / centriolar subdistal appendage ...Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / intracellular transport of viral protein in host cell / secretory vesicle / positive regulation of neuromuscular junction development / centriolar subdistal appendage / positive regulation of non-motile cilium assembly / centriole-centriole cohesion / transport along microtubule / intraciliary retrograde transport / dynein light chain binding / ventral spinal cord development / microtubule anchoring at centrosome / mitocytosis / motile cilium assembly / dynein heavy chain binding / positive regulation of intracellular transport / regulation of metaphase plate congression / establishment of spindle localization / Activation of BIM and translocation to mitochondria / melanosome transport / ciliary tip / positive regulation of spindle assembly / retromer complex / nuclear membrane disassembly / microtubule plus-end / positive regulation of microtubule nucleation / Intraflagellar transport / negative regulation of nitric oxide biosynthetic process / negative regulation of phosphorylation / P-body assembly / dynein complex / COPI-independent Golgi-to-ER retrograde traffic / regulation of G protein-coupled receptor signaling pathway / microtubule-dependent intracellular transport of viral material towards nucleus / minus-end-directed microtubule motor activity / cytoplasmic dynein complex / retrograde axonal transport / non-motile cilium assembly / dynein light intermediate chain binding / Recruitment of NuMA to mitotic centrosomes / host cell / enzyme inhibitor activity / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / COPI-independent Golgi-to-ER retrograde traffic / MHC class II antigen presentation / retrograde transport, endosome to Golgi / nuclear migration / COPI-mediated anterograde transport / microtubule associated complex / motor behavior / centrosome localization / neuromuscular process / microtubule motor activity / Macroautophagy / dynein intermediate chain binding / neuromuscular junction development / intercellular bridge / microtubule-based movement / cell leading edge / spermatid development / positive regulation of insulin secretion involved in cellular response to glucose stimulus / establishment of mitotic spindle orientation / tertiary granule membrane / ficolin-1-rich granule membrane / cytoplasmic microtubule / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / COPI-mediated anterograde transport / stress granule assembly / cytoplasmic microtubule organization / Mitotic Prometaphase / regulation of mitotic spindle organization / EML4 and NUDC in mitotic spindle formation / axon cytoplasm / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Resolution of Sister Chromatid Cohesion / Recruitment of NuMA to mitotic centrosomes / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Anchoring of the basal body to the plasma membrane / substantia nigra development / MHC class II antigen presentation / neuron projection maintenance / centriole / nitric-oxide synthase regulator activity / AURKA Activation by TPX2 / cellular response to nerve growth factor stimulus / mitotic spindle organization / ciliary basal body / regulation of mitochondrial membrane potential / filopodium / RHO GTPases Activate Formins / cilium / mitotic spindle / spindle Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) Sus scrofa (pig) | ||||||||||||
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: 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
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-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 (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-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: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q13409 #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: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q14204 #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: Spodoptera frugiperda (fall armyworm) / References: UniProt: O43237 |
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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: Spodoptera frugiperda (fall armyworm) / References: UniProt: P63167 #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: Spodoptera frugiperda (fall armyworm) / References: UniProt: P63172 |
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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) Sus scrofa (pig) / References: UniProt: A0A287B8J2 |
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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 |
-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: Spodoptera frugiperda (fall armyworm) |
Buffer solution | pH: 7.2 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-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 FIELDBright-field microscopy / 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) |
-Processing
EM software |
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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 |