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Yorodumi- PDB-9yne: Motor domain of human dynein-1 in pre-power stroke bound to dynac... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9yne | ||||||||||||||||||||||||||||||
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| Title | Motor domain of human dynein-1 in pre-power stroke bound to dynactin-p150glued-CC1B-ICD and LIS1 | ||||||||||||||||||||||||||||||
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Keywords | MOTOR PROTEIN / Dynein-1 / Lis1 / p150glued | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationintracellular transport of viral protein in host cell / nitric-oxide synthase inhibitor activity / cell cortex region / microtubule cytoskeleton organization involved in establishment of planar polarity / establishment of planar polarity of embryonic epithelium / 1-alkyl-2-acetylglycerophosphocholine esterase complex / negative regulation of DNA strand resection involved in replication fork processing / secretory vesicle / corpus callosum morphogenesis / centriolar subdistal appendage ...intracellular transport of viral protein in host cell / nitric-oxide synthase inhibitor activity / cell cortex region / microtubule cytoskeleton organization involved in establishment of planar polarity / establishment of planar polarity of embryonic epithelium / 1-alkyl-2-acetylglycerophosphocholine esterase complex / negative regulation of DNA strand resection involved in replication fork processing / secretory vesicle / corpus callosum morphogenesis / centriolar subdistal appendage / negative regulation of phosphorylation / maintenance of centrosome location / ameboidal-type cell migration / positive regulation of neuromuscular junction development / centriole-centriole cohesion / intraciliary retrograde transport / platelet activating factor metabolic process / radial glia-guided pyramidal neuron migration / microtubule anchoring at centrosome / establishment of centrosome localization / central region of growth cone / cerebral cortex neuron differentiation / acrosome assembly / nuclear membrane disassembly / maintenance of synapse structure / microtubule sliding / dynein light chain binding / transport along microtubule / ventral spinal cord development / dynein heavy chain binding / Activation of BIM and translocation to mitochondria / positive regulation of cytokine-mediated signaling pathway / motile cilium assembly / positive regulation of embryonic development / microtubule organizing center organization / interneuron migration / layer formation in cerebral cortex / mitotic nuclear membrane disassembly / dynein complex / astral microtubule / auditory receptor cell development / microtubule plus-end / cortical microtubule organization / XBP1(S) activates chaperone genes / positive regulation of microtubule nucleation / Intraflagellar transport / myeloid leukocyte migration / reelin-mediated signaling pathway / positive regulation of intracellular transport / regulation of metaphase plate congression / positive regulation of spindle assembly / positive regulation of dendritic spine morphogenesis / negative regulation of nitric oxide biosynthetic process / melanosome transport / establishment of spindle localization / osteoclast development / regulation of G protein-coupled receptor signaling pathway / stereocilium / microtubule plus-end binding / microtubule-dependent intracellular transport of viral material towards nucleus / brain morphogenesis / non-motile cilium assembly / motile cilium / vesicle transport along microtubule / retrograde transport, endosome to Golgi / retrograde axonal transport / COPI-independent Golgi-to-ER retrograde traffic / P-body assembly / minus-end-directed microtubule motor activity / microtubule associated complex / negative regulation of JNK cascade / centrosome localization / dynein light intermediate chain binding / cytoplasmic dynein complex / microtubule motor activity / kinesin complex / neuromuscular process controlling balance / stem cell division / microtubule-based movement / nuclear migration / perinuclear theca / neuromuscular process / Macroautophagy / establishment of mitotic spindle orientation / neuromuscular junction development / dynein intermediate chain binding / germ cell development / motor behavior / cell leading edge / transmission of nerve impulse / dynein complex binding / tertiary granule membrane / neuroblast proliferation / dynactin binding / cochlea development / ficolin-1-rich granule membrane / protein secretion / spermatid development / positive regulation of axon extension / microtubule-based process Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 8.46 Å | ||||||||||||||||||||||||||||||
Authors | Yang, J. / Rao, Q. / Chai, P. / Zhang, K. | ||||||||||||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: Nature / Year: 2026Title: Roles of microtubules and LIS1 in dynein transport machinery assembly. Authors: Qinhui Rao / Jun Yang / Pengxin Chai / Steven Markus / Kai Zhang / ![]() Abstract: Cytoplasmic dynein-1, a microtubule (MT)-based motor protein, requires dynactin and a coiled-coil adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The roles of MTs and dynein ...Cytoplasmic dynein-1, a microtubule (MT)-based motor protein, requires dynactin and a coiled-coil adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The roles of MTs and dynein regulator lissencephaly-1 (LIS1) in DDA assembly have remained elusive. Here we use cryo-electron microscopy to determine the structural basis of MT- and LIS1-mediated DDA assembly. We show that an adaptor-independent dynein-dynactin complex spontaneously forms on MTs with an intrinsic 2:1 stoichiometry in a highly efficient manner, driven by parallel alignment of dynein tails upon MT binding. Adaptors can wedge into and exchange within the assembled MT-bound dynein-dynactin complex; these processes are enabled by relative rotations between dynein and dynactin and facilitated by the dynein light-intermediate chains that assist the adaptor 'search' mechanism. Although LIS1 is dispensable for efficient DD(A)-MT assembly, its presence expands the conformational landscape of DD(A) assemblies on MTs. Cryo-electron microscopy reveals that LIS1 bridges dynactin p150 and dynein in both the closed Phi-like and open prepowerstroke states, stabilizing low-MT-affinity intermediates that tether dynein molecules in proximity to MTs and prime them for subsequent DD(A) assembly through alternative pathways. These findings demonstrate the dynamic adaptability of the dynein transport machinery and the coordinated roles of MTs and LIS1 in DDA assembly. | ||||||||||||||||||||||||||||||
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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 | 9yne.cif.gz | 903.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9yne.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9yne.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yn/9yne ftp://data.pdbj.org/pub/pdb/validation_reports/yn/9yne | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 73175MC ![]() 9dgpC ![]() 9dgqC ![]() 9dgrC ![]() 9dgsC ![]() 9dgtC ![]() 9dguC ![]() 9dgvC ![]() 9yncC ![]() 9yndC ![]() 9ynfC ![]() 9yngC ![]() 9ynhC 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, 4 molecules ADEu
| #1: Protein | Mass: 533083.250 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325 / Production host: ![]() | ||
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| #3: Protein | Mass: 71546.445 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: ![]() #7: Protein | | Mass: 54173.156 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: ![]() |
-Protein , 2 types, 4 molecules BCFG
| #2: Protein | Mass: 46709.984 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PAFAH1B1, LIS1, MDCR, MDS, PAFAHA / Production host: ![]() #4: Protein | Mass: 142015.484 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DCTN1 / Production host: ![]() |
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-Dynein light chain ... , 2 types, 4 molecules dikv
| #5: 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: ![]() #6: 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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-Non-polymers , 3 types, 6 molecules 




| #8: Chemical | | #9: Chemical | #10: Chemical | ChemComp-ATP / | |
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-Details
| Has ligand of interest | Y |
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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: Motor domain of human dynein-1 in pre-power stroke bound to dynactin-p150glued-CC1B-ICD and LIS1 Type: COMPLEX / Entity ID: #1-#7 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.2 |
| Specimen | Conc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Microscopy | Model: TFS GLACIOS |
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| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 45000 X / Calibrated magnification: 45000 X / Nominal defocus max: 2600 nm / Nominal defocus min: 1200 nm / Calibrated defocus min: 1200 nm / Calibrated defocus max: 2600 nm / Cs: 2.7 mm / C2 aperture diameter: 30 µm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
| 3D reconstruction | Resolution: 8.46 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 52203 / Symmetry type: POINT |
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About Yorodumi



Homo sapiens (human)
United States, 1items
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FIELD EMISSION GUN