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Yorodumi- PDB-9mfy: Motor domain-Pac1 complex with ADP AAA1 and Apo AAA3 from yeast f... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9mfy | ||||||||||||||||||||||||||||||
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| Title | Motor domain-Pac1 complex with ADP AAA1 and Apo AAA3 from yeast full-length dynein-1 and Pac1 in 0.1 mM ATP condition | ||||||||||||||||||||||||||||||
Components |
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Keywords | MOTOR PROTEIN / dynein | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationmicrotubule sliding / karyogamy / microtubule organizing center organization / nuclear migration along microtubule / astral microtubule / establishment of mitotic spindle localization / microtubule plus-end binding / spindle pole body / vesicle transport along microtubule / microtubule associated complex ...microtubule sliding / karyogamy / microtubule organizing center organization / nuclear migration along microtubule / astral microtubule / establishment of mitotic spindle localization / microtubule plus-end binding / spindle pole body / vesicle transport along microtubule / microtubule associated complex / minus-end-directed microtubule motor activity / dynein light intermediate chain binding / cytoplasmic dynein complex / nuclear migration / dynein intermediate chain binding / dynein complex binding / establishment of mitotic spindle orientation / Antigen processing: Ubiquitination & Proteasome degradation / mitotic sister chromatid segregation / cytoplasmic microtubule / cytoplasmic microtubule organization / Neutrophil degranulation / mitotic spindle organization / kinetochore / spindle pole / nuclear envelope / cell cortex / cell division / ATP hydrolysis activity / ATP binding / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||||||||||||||||||||||||||
Authors | Geohring, I.C. / Chai, P. / Iyer, B.R. | ||||||||||||||||||||||||||||||
| Funding support | United States, 2items
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Citation | Journal: To Be PublishedTitle: A nucleotide code governs Lis1's ability to relieve dynein autoinhibition Authors: Geohring, I.C. / Chai, P. / Iyer, B.R. | ||||||||||||||||||||||||||||||
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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 | 9mfy.cif.gz | 566.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9mfy.ent.gz | 438.1 KB | Display | PDB format |
| PDBx/mmJSON format | 9mfy.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9mfy_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
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| Full document | 9mfy_full_validation.pdf.gz | 1.8 MB | Display | |
| Data in XML | 9mfy_validation.xml.gz | 93.5 KB | Display | |
| Data in CIF | 9mfy_validation.cif.gz | 140.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mf/9mfy ftp://data.pdbj.org/pub/pdb/validation_reports/mf/9mfy | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 48242MC ![]() 9mfvC ![]() 9mfwC ![]() 9mfxC 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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| 1 |
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Components
| #1: Protein | Mass: 56973.562 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: PAC1, LIS1, YOR269W / Production host: ![]() | ||||||||
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| #2: Protein | Mass: 471918.750 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: DYN1, DHC1, YKR054C / Production host: ![]() | ||||||||
| #3: Chemical | | #4: Chemical | ChemComp-ATP / | #5: Chemical | Has ligand of interest | Y | 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-Pac1 complex with ADP AAA1 and Apo AAA3 from yeast full-length dynein-1 and Pac1 in 0.1 mM ATP condition Type: COMPLEX / Details: class2, ADP AAA1, Apo AAA3, with Pac1 bound / Entity ID: #1-#2 / Source: RECOMBINANT |
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| Molecular weight | Value: 1.2 MDa / Experimental value: YES |
| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| 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: 2500 nm / Nominal defocus min: 1200 nm / Calibrated defocus min: 1200 nm / Calibrated defocus max: 2500 nm / Cs: 2.7 mm / C2 aperture diameter: 100 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: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 178195 / Algorithm: BACK PROJECTION / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.3 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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United States, 2items
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FIELD EMISSION GUN