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Yorodumi- PDB-9dgs: Dynactin and dynein tail region of dynein-dynactin complex on mic... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9dgs | |||||||||||||||||||||||||||
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| Title | Dynactin and dynein tail region of dynein-dynactin complex on microtubules | |||||||||||||||||||||||||||
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Keywords | MOTOR PROTEIN / dynein / dynactin / microtubule | |||||||||||||||||||||||||||
| Function / homology | Function and homology information: / Factors involved in megakaryocyte development and platelet production / retrograde axonal transport of mitochondrion / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions / RHO GTPases Activate WASPs and WAVEs / MAP2K and MAPK activation ...: / Factors involved in megakaryocyte development and platelet production / retrograde axonal transport of mitochondrion / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions / RHO GTPases Activate WASPs and WAVEs / MAP2K and MAPK activation / Formation of the canonical BAF (cBAF) complex / Formation of the polybromo-BAF (pBAF) complex / Formation of the embryonic stem cell BAF (esBAF) complex / Formation of the non-canonical BAF (ncBAF) complex / UCH proteinases / Gap junction degradation / Formation of annular gap junctions / RHOF GTPase cycle / Clathrin-mediated endocytosis / Regulation of CDH1 Function / Formation of the dystrophin-glycoprotein complex (DGC) / dynactin complex / centriolar subdistal appendage / positive regulation of neuromuscular junction development / centriole-centriole cohesion / 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 / Recruitment of mitotic centrosome proteins and complexes / microtubule anchoring at centrosome / nuclear membrane disassembly / F-actin capping protein complex / WASH complex / ventral spinal cord development / cytoskeleton-dependent cytokinesis / retromer complex / microtubule plus-end / dynein complex / cellular response to cytochalasin B / positive regulation of microtubule nucleation / regulation of transepithelial transport / morphogenesis of a polarized epithelium / structural constituent of postsynaptic actin cytoskeleton / melanosome transport / protein localization to adherens junction / barbed-end actin filament capping / dense body / Tat protein binding / Neutrophil degranulation / coronary vasculature development / postsynaptic actin cytoskeleton / non-motile cilium assembly / regulation of cell morphogenesis / adherens junction assembly / retrograde transport, endosome to Golgi / apical protein localization / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / minus-end-directed microtubule motor activity / Recruitment of NuMA to mitotic centrosomes / microtubule associated complex / tight junction / cytoplasmic dynein complex / dynein light intermediate chain binding / COPI-mediated anterograde transport / ventricular septum development / aorta development / microtubule-based movement / nuclear migration / apical junction complex / neuromuscular process / regulation of norepinephrine uptake / transporter regulator activity / establishment of mitotic spindle orientation / neuromuscular junction development / NuA4 histone acetyltransferase complex / dynein intermediate chain binding / motor behavior / establishment or maintenance of cell polarity / cell leading edge / cortical cytoskeleton / cleavage furrow / dynein complex binding / microtubule organizing center / nitric-oxide synthase binding / brush border / regulation of synaptic vesicle endocytosis / kinesin binding / regulation of protein localization to plasma membrane / positive regulation of double-strand break repair via homologous recombination / intercellular bridge / stress fiber / axon cytoplasm / neuron projection maintenance / cytoskeleton organization / axonogenesis Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å | |||||||||||||||||||||||||||
Authors | Rao, Q. / Chai, P. / Zhang, K. | |||||||||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: bioRxiv / Year: 2024Title: Molecular basis for the assembly of the dynein transport machinery on microtubules. Authors: Qinhui Rao / Pengxin Chai / Kai Zhang / ![]() Abstract: Cytoplasmic dynein-1, a microtubule-based motor protein, requires dynactin and an adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The role of microtubules in DDA assembly has ...Cytoplasmic dynein-1, a microtubule-based motor protein, requires dynactin and an adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The role of microtubules in DDA assembly has been elusive. Here, we reveal detailed structural insights into microtubule-mediated DDA assembly using cryo-electron microscopy. We find that an adaptor-independent dynein-dynactin complex (DD) predominantly forms on microtubules in an intrinsic 2:1 stoichiometry, induced by spontaneous parallelization of dynein upon microtubule binding. Adaptors can squeeze in and exchange within the assembled microtubule-bound DD complex, which is enabled by relative rotations between dynein and dynactin, and further facilitated by dynein light intermediate chains that assist in an adaptor 'search' mechanism. Our findings elucidate the dynamic adaptability of the dynein transport machinery, and reveal a new mode for assembly of the motile complex. | |||||||||||||||||||||||||||
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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 | 9dgs.cif.gz | 2.2 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9dgs.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9dgs.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dg/9dgs ftp://data.pdbj.org/pub/pdb/validation_reports/dg/9dgs | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 46846MC ![]() 9dgpC ![]() 9dgqC ![]() 9dgrC ![]() 9dgtC ![]() 9dguC ![]() 9dgvC 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
-Protein , 3 types, 10 molecules ABCDEFGIHJ
| #1: Protein | Mass: 42670.688 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | | Mass: 41782.660 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q6QAQ1, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement #3: Protein | | Mass: 46250.785 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-F-actin-capping protein subunit ... , 2 types, 2 molecules KL
| #4: Protein | Mass: 33059.848 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #5: Protein | Mass: 30669.768 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Dynactin subunit ... , 6 types, 11 molecules MNPQORUVWZY
| #6: Protein | Mass: 44704.414 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 21192.477 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | | Mass: 20703.910 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | | Mass: 20150.533 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 142015.484 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | | Mass: 52920.434 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Cytoplasmic dynein 1 ... , 2 types, 8 molecules efmnghop
| #12: Protein | Mass: 532739.562 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 68567.219 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 3 types, 13 molecules 




| #14: Chemical | ChemComp-ADP / #15: Chemical | ChemComp-ATP / | #16: Chemical | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-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: Dynactin and dynein tail region of dynein-dynactin complex on microtubules Type: COMPLEX / Entity ID: #1-#13 / Source: NATURAL |
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| Molecular weight | Value: 5 MDa / Experimental value: NO |
| Source (natural) | 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 1200 nm / Calibrated defocus min: 1200 nm / Calibrated defocus max: 3000 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 62404 / Symmetry type: POINT |
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