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Open data
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Basic information
Entry | Database: PDB / ID: 9.0E+28 | |||||||||||||||||||||||||||
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Title | Cryo-EM structure of Phi dynein tail | |||||||||||||||||||||||||||
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![]() | MOTOR PROTEIN / human / complex | |||||||||||||||||||||||||||
Function / homology | ![]() intracellular transport of viral protein in host cell / secretory vesicle / deoxyribonuclease inhibitor activity / negative regulation of DNA strand resection involved in replication fork processing / transport along microtubule / intraciliary retrograde transport / visual behavior / dynein light chain binding / dynein heavy chain binding / motile cilium assembly ...intracellular transport of viral protein in host cell / secretory vesicle / deoxyribonuclease inhibitor activity / negative regulation of DNA strand resection involved in replication fork processing / transport along microtubule / intraciliary retrograde transport / visual behavior / dynein light chain binding / dynein heavy chain binding / motile cilium assembly / Activation of BIM and translocation to mitochondria / negative regulation of phosphorylation / ciliary tip / Intraflagellar transport / positive regulation of intracellular transport / regulation of metaphase plate congression / establishment of spindle localization / positive regulation of spindle assembly / 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 / minus-end-directed microtubule motor activity / P-body assembly / microtubule motor activity / dynein light intermediate chain binding / cytoplasmic dynein complex / centrosome localization / dynein intermediate chain binding / nuclear migration / microtubule-based movement / Macroautophagy / establishment of mitotic spindle orientation / enzyme inhibitor activity / tertiary granule membrane / ficolin-1-rich granule membrane / cytoplasmic microtubule / COPI-mediated anterograde transport / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / cytoplasmic microtubule organization / axon cytoplasm / Mitotic Prometaphase / substantia nigra development / 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 / Recruitment of mitotic centrosome proteins and complexes / MHC class II antigen presentation / Recruitment of NuMA to mitotic centrosomes / regulation of mitotic spindle organization / Anchoring of the basal body to the plasma membrane / Resolution of Sister Chromatid Cohesion / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / AURKA Activation by TPX2 / mitotic spindle organization / filopodium / RHO GTPases Activate Formins / cellular response to nerve growth factor stimulus / kinetochore / negative regulation of neurogenesis / spindle / microtubule cytoskeleton organization / 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 / cell cortex / secretory granule lumen / vesicle / microtubule / ficolin-1-rich granule lumen / cytoskeleton / cilium / symbiont entry into host cell / cell division / apoptotic process / centrosome / DNA damage response / Neutrophil degranulation / Golgi apparatus / ATP hydrolysis activity / mitochondrion / RNA binding / extracellular exosome / extracellular region / ATP binding / identical protein binding / nucleus / membrane / plasma membrane / cytosol Similarity search - Function | |||||||||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.4 Å | |||||||||||||||||||||||||||
![]() | Nguyen, K.H.V. / Kendrick, A.A. / Leschziner, A.E. | |||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of Pre-Chi dynein bound to Lis1 Authors: Nguyen, K.H.V. / Kendrick, A.A. / Leschziner, A.E. | |||||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 961.2 KB | Display | ![]() |
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PDB format | ![]() | 510.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.8 MB | Display | ![]() |
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Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 97 KB | Display | |
Data in CIF | ![]() | 165 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 47443MC ![]() 9dzyC ![]() 9e0kC ![]() 9e0tC ![]() 9e0uC ![]() 9e0wC ![]() 9e0xC ![]() 9e0yC ![]() 9e22C ![]() 9e23C C: citing same article ( M: map data used to model this data |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Cytoplasmic dynein 1 ... , 2 types, 6 molecules AGefBC
#1: Protein | Mass: 554126.250 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 54173.156 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Protein , 1 types, 4 molecules DHgh
#3: Protein | Mass: 68442.141 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Dynein light chain ... , 3 types, 6 molecules EFdikv
#4: Protein | Mass: 10934.576 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #5: Protein | Mass: 10381.899 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #6: Protein | Mass: 12461.996 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Details
Has protein modification | N |
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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: Human Cytoplasmic dynein-1 / Type: COMPLEX / Entity ID: #4, #3, #5-#6, #2, #1 / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Instrument: HOMEMADE PLUNGER / Cryogen name: ETHANE-PROPANE |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3250 nm / Nominal defocus min: 610 nm |
Image recording | Electron dose: 55 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 21400 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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