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Yorodumi- PDB-9bly: Composite structure of full-length human dynein-1 in phi-particle... -
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Basic information
| Entry | Database: PDB / ID: 9bly | ||||||||||||||||||||||||||||||||||||||||||
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| Title | Composite structure of full-length human dynein-1 in phi-particle conformation | ||||||||||||||||||||||||||||||||||||||||||
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Keywords | MOTOR PROTEIN / dynein-1 / phi-particle | ||||||||||||||||||||||||||||||||||||||||||
| 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: 3.5 Å | ||||||||||||||||||||||||||||||||||||||||||
Authors | Chai, P. / Zhang, K. | ||||||||||||||||||||||||||||||||||||||||||
| Funding support | United States, 2items
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Citation | Journal: Nat Struct Mol Biol / Year: 2025Title: The mechanochemical cycle of reactive full-length human dynein 1. Authors: Pengxin Chai / Jun Yang / Indigo C Geohring / Steven M Markus / Yue Wang / Kai Zhang / ![]() Abstract: Dynein-driven cargo transport has a pivotal role in diverse cellular activities, central to which is dynein's mechanochemical cycle. Here, we performed a systematic cryo-electron microscopic ...Dynein-driven cargo transport has a pivotal role in diverse cellular activities, central to which is dynein's mechanochemical cycle. Here, we performed a systematic cryo-electron microscopic investigation of the conformational landscape of full-length human dynein 1 in reaction, in various nucleotide conditions, on and off microtubules. Our approach reveals over 40 high-resolution structures, categorized into eight states, providing a dynamic and comprehensive view of dynein throughout its mechanochemical cycle. The described intermediate states reveal mechanistic insights into dynein function, including a 'backdoor' phosphate release model that coordinates linker straightening, how microtubule binding enhances adenosine triphosphatase activity through a two-way communication mechanism and the crosstalk mechanism between AAA1 and the regulatory AAA3 site. Our findings also lead to a revised model for the force-generating powerstroke and reveal means by which dynein exhibits unidirectional stepping. These results improve our understanding of dynein and provide a more complete model of its mechanochemical cycle. | ||||||||||||||||||||||||||||||||||||||||||
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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 | 9bly.cif.gz | 2 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9bly.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9bly.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9bly_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 9bly_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 9bly_validation.xml.gz | 279.9 KB | Display | |
| Data in CIF | 9bly_validation.cif.gz | 434.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bl/9bly ftp://data.pdbj.org/pub/pdb/validation_reports/bl/9bly | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 44681MC ![]() 9blzC ![]() 9bm0C ![]() 9bm1C ![]() 9bm2C ![]() 9bm3C ![]() 9bm4C ![]() 9bm5C ![]() 9bm6C ![]() 9bm7C ![]() 9bm8C ![]() 9bmaC ![]() 9bmbC ![]() 9bmcC ![]() 9bmdC ![]() 9bmfC ![]() 9bmgC ![]() 9bmhC ![]() 9bmjC ![]() 9bmlC ![]() 9bmmC ![]() 9bmnC ![]() 9bmoC ![]() 9bmpC ![]() 9bmrC ![]() 9bmsC ![]() 9bmtC ![]() 9bmuC ![]() 9bmvC ![]() 9bmwC ![]() 9bmyC ![]() 9bmzC ![]() 9bn0C ![]() 9bn1C ![]() 9bn3C ![]() 9bn4C ![]() 9bn5C ![]() 9bn6C ![]() 9dh5C ![]() 9dh6C ![]() 9dh7C ![]() 9dh8C ![]() 9dh9C ![]() 9dhaC 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, 6 molecules ABCDEF
| #1: Protein | Mass: 533083.250 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325 / Production host: ![]() #2: 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: ![]() #3: 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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-Dynein light chain ... , 3 types, 6 molecules GHIJKL
| #4: 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: ![]() #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, 12 molecules 




| #7: Chemical | ChemComp-ADP / #8: Chemical | #9: Chemical | ChemComp-MG / |
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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: full-length human dynein-1 in phi-particle conformation Type: COMPLEX / Entity ID: #1-#6 / Source: RECOMBINANT |
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| Molecular weight | Value: 1.5 MDa / Experimental value: YES |
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.2 Details: 25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ATP |
| Specimen | Conc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/1 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 278 K |
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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 magnification: 105000 X / Calibrated magnification: 105000 X / Nominal defocus max: 5000 nm / Nominal defocus min: 1200 nm / Calibrated defocus min: 3000 nm / Calibrated defocus max: 3000 nm / Cs: 2.7 mm / C2 aperture diameter: 50 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: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 57816 / Symmetry type: POINT |
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Homo sapiens (human)
United States, 2items
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FIELD EMISSION GUN