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Open data
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Basic information
| Entry | Database: PDB / ID: 7fj3 | ||||||
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| Title | Cryo-EM structure of PRV A-capid | ||||||
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Keywords | VIRUS / Pseudorabies virus / C-capsid / Cryo-EM | ||||||
| Function / homology | Function and homology informationT=16 icosahedral viral capsid / viral capsid assembly / viral process / viral capsid / host cell nucleus / structural molecule activity / DNA binding Similarity search - Function | ||||||
| Biological species | ![]() Suid alphaherpesvirus 1 | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.53 Å | ||||||
Authors | Zheng, Q. / Li, S. / Zha, Z. / Sun, H. | ||||||
| Funding support | 1items
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Citation | Journal: Nat Commun / Year: 2022Title: Structures of pseudorabies virus capsids. Authors: Guosong Wang / Zhenghui Zha / Pengfei Huang / Hui Sun / Yang Huang / Maozhou He / Tian Chen / Lina Lin / Zhenqin Chen / Zhibo Kong / Yuqiong Que / Tingting Li / Ying Gu / Hai Yu / Jun Zhang ...Authors: Guosong Wang / Zhenghui Zha / Pengfei Huang / Hui Sun / Yang Huang / Maozhou He / Tian Chen / Lina Lin / Zhenqin Chen / Zhibo Kong / Yuqiong Que / Tingting Li / Ying Gu / Hai Yu / Jun Zhang / Qingbing Zheng / Yixin Chen / Shaowei Li / Ningshao Xia / ![]() Abstract: Pseudorabies virus (PRV) is a major etiological agent of swine infectious diseases and is responsible for significant economic losses in the swine industry. Recent data points to human viral ...Pseudorabies virus (PRV) is a major etiological agent of swine infectious diseases and is responsible for significant economic losses in the swine industry. Recent data points to human viral encephalitis caused by PRV infection, suggesting that PRV may be able to overcome the species barrier to infect humans. To date, there is no available therapeutic for PRV infection. Here, we report the near-atomic structures of the PRV A-capsid and C-capsid, and illustrate the interaction that occurs between these subunits. We show that the C-capsid portal complex is decorated with capsid-associated tegument complexes. The PRV capsid structure is highly reminiscent of other α-herpesviruses, with some additional structural features of β- and γ-herpesviruses. These results illustrate the structure of the PRV capsid and elucidate the underlying assembly mechanism at the molecular level. This knowledge may be useful for the development of oncolytic agents or specific therapeutics against this arm of the herpesvirus family. | ||||||
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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 | 7fj3.cif.gz | 4.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7fj3.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7fj3.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7fj3_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
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| Full document | 7fj3_full_validation.pdf.gz | 1.9 MB | Display | |
| Data in XML | 7fj3_validation.xml.gz | 572.6 KB | Display | |
| Data in CIF | 7fj3_validation.cif.gz | 912.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fj/7fj3 ftp://data.pdbj.org/pub/pdb/validation_reports/fj/7fj3 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 31612MC ![]() 7fj1C 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 | x 60![]()
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| 2 |
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| 3 | x 5![]()
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| 4 | x 6![]()
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| 5 | ![]()
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| Symmetry | Point symmetry: (Schoenflies symbol: I (icosahedral)) |
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Components
| #1: Protein | Mass: 146101.984 Da / Num. of mol.: 16 / Source method: isolated from a natural source / Source: (natural) ![]() Suid alphaherpesvirus 1 / References: UniProt: G3G8T2#2: Protein | Mass: 31763.766 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) ![]() Suid alphaherpesvirus 1 / References: UniProt: G3G8T3#3: Protein | Mass: 40008.594 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) ![]() Suid alphaherpesvirus 1 / References: UniProt: Q85211#4: Protein | Mass: 11509.209 Da / Num. of mol.: 15 / Source method: isolated from a natural source / Source: (natural) ![]() Suid alphaherpesvirus 1 / References: UniProt: G3G8R4Has protein modification | Y | |
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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: Cryo-EM structure of PRV A-capsid / Type: VIRUS / Entity ID: all / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() Suid alphaherpesvirus 1 |
| Details of virus | Empty: NO / Enveloped: YES / Isolate: OTHER / Type: VIRION |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Tecnai F30 / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TECNAI F30 |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
| Software | Name: UCSF ChimeraX / Version: 1.3/v9 / Classification: model building / URL: https://www.rbvi.ucsf.edu/chimerax/ / Os: Linux / Type: package |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3D reconstruction | Resolution: 4.53 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 8899 / Symmetry type: POINT |
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Suid alphaherpesvirus 1
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FIELD EMISSION GUN