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Open data
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Basic information
Entry | Database: PDB / ID: 8fjk | |||||||||||||||||||||
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Title | Golden Shiner Reovirus Core Polar Vertex | |||||||||||||||||||||
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![]() | VIRUS / dsRNA / RNA-dependent / RNA-polymerase | |||||||||||||||||||||
Function / homology | ![]() viral intermediate capsid / T=2 icosahedral viral capsid / viral inner capsid / host cytoskeleton / viral outer capsid / 7-methylguanosine mRNA capping / viral genome replication / mRNA guanylyltransferase activity / mRNA guanylyltransferase / mRNA (guanine-N7)-methyltransferase ...viral intermediate capsid / T=2 icosahedral viral capsid / viral inner capsid / host cytoskeleton / viral outer capsid / 7-methylguanosine mRNA capping / viral genome replication / mRNA guanylyltransferase activity / mRNA guanylyltransferase / mRNA (guanine-N7)-methyltransferase / viral nucleocapsid / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / host cell cytoplasm / RNA helicase activity / hydrolase activity / RNA helicase / RNA-directed RNA polymerase / RNA-dependent RNA polymerase activity / nucleotide binding / GTP binding / structural molecule activity / ATP hydrolysis activity / RNA binding / ATP binding / metal ion binding Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||||||||||||||
![]() | Stevens, A.S. / Zhou, Z.H. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Asymmetric reconstruction of the aquareovirus core at near-atomic resolution and mechanism of transcription initiation. Authors: Alexander Stevens / Yanxiang Cui / Sakar Shivakoti / Z Hong Zhou / ![]() | |||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 4.1 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 29243MC ![]() 8fjlC 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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1 |
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Components
-Protein , 4 types, 17 molecules ABVWXabdeghnYZcfi
#1: Protein | Mass: 141605.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||
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#2: Protein | Mass: 79347.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||
#5: Protein | Mass: 44489.391 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 141109.750 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q8JU62, mRNA guanylyltransferase, mRNA (guanine-N7)-methyltransferase |
-Major inner capsid protein ... , 2 types, 15 molecules CDEFGHIJKLMNklm
#3: Protein | Mass: 124694.531 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 9147.655 Da / Num. of mol.: 5 / Fragment: N-terminal residues 13-106 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-RNA chain , 6 types, 12 molecules a1b1a2b2a3b3a4b4a5b5a6b6
#7: RNA chain | Mass: 16474.699 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #8: RNA chain | Mass: 19016.188 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: RNA chain | Mass: 12662.472 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #10: RNA chain | Mass: 5673.388 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #11: RNA chain | Mass: 12027.101 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #12: RNA chain | Mass: 9485.617 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 1 types, 4 molecules ![](data/chem/img/ZN.gif)
#13: Chemical | ChemComp-ZN / |
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-Details
Has ligand of interest | 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: Golden shiner reovirus / Type: VIRUS Details: cultured in Fat Head minnow cellsfrom ATCC "CCL-42" Entity ID: #1-#12 / Source: NATURAL |
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Molecular weight | Value: 47 MDa / Experimental value: NO |
Source (natural) | Organism: ![]() |
Details of virus | Empty: NO / Enveloped: NO / Isolate: SPECIES / Type: VIRION |
Natural host | Organism: Notemigonus crysoleucas |
Virus shell | Name: inner capsid shell |
Buffer solution | pH: 7.4 / Details: Phosphate buffered saline |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES Details: The sample was acquired from the media of infected cell culture |
Specimen support | Grid type: Quantifoil R2/1 |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 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: ![]() |
Electron lens | Mode: BRIGHT FIELD / Calibrated magnification: 81000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 1500 nm / Calibrated defocus min: 1500 nm / Calibrated defocus max: 2500 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: 45 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
EM software |
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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: 119182 / Symmetry type: POINT |