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Open data
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Basic information
Entry | Database: PDB / ID: 9fhp | |||||||||
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Title | CryoEM structure of wild-type Turnip Yellows Virus | |||||||||
![]() | Minor capsid readthrough protein | |||||||||
![]() | VIRUS / read-through protein | |||||||||
Function / homology | Potato leaf roll virus readthrough protein / Potato leaf roll virus readthrough protein / Luteovirus group 1 coat protein / Luteovirus coat protein / host cell plasmodesma / host cell periplasmic space / viral capsid / structural molecule activity / Readthrough protein P3-RTD![]() | |||||||||
Biological species | ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.08 Å | |||||||||
![]() | Trapani, S. / Lai Kee Him, J. / Hoh, F. / Brault, V. / Bron, P. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of the turnip yellows virus particles. Authors: Joséphine Lai-Kee-Him / Stefano Trapani / Sylvaine Boissinot / Catherine Reinbold / Chloé Fallet / Aurélie Ancelin / François Lecorre / François Hoh / Véronique Ziegler-Graff / ...Authors: Joséphine Lai-Kee-Him / Stefano Trapani / Sylvaine Boissinot / Catherine Reinbold / Chloé Fallet / Aurélie Ancelin / François Lecorre / François Hoh / Véronique Ziegler-Graff / Véronique Brault / Patrick Bron / ![]() Abstract: Turnip yellows virus (TuYV) is a plant virus infecting important crops such as oilseed rape. TuYV is phloem-restricted and transmitted by aphids. The capsid contains two subunit types: the major ...Turnip yellows virus (TuYV) is a plant virus infecting important crops such as oilseed rape. TuYV is phloem-restricted and transmitted by aphids. The capsid contains two subunit types: the major capsid protein (CP) and a minor component (RTP∗) which arises from the C-terminal cleavage of a readthrough product (RTP). RTP∗ contains the CP sequence fused with a structured domain, denoted RTD, which is a key determinant of virus transmission. Though both CP and RTP∗ are involved in virus movement and aphid transmission, how RTP∗ is incorporated into the capsid is poorly understood. We present here the structural characterisation, by immunogold labelling and 3D cryo-EM, of the wild-type TuYV and a mutant whose capsid contains the CP only. We show that incorporation of RTP∗ does not impair the capsid structure, and the RTD does not adopt well-defined positions at the capsid surface. The number of incorporated RTP∗s suggests a random insertion. | |||||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.9 KB | Display | ![]() |
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PDB format | ![]() | 62.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 10003MC ![]() 9q8jC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
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Components
#1: Protein | Mass: 22522.520 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() 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: Turnip yellows virus / Type: VIRUS / Details: agroiniltration (English et al. 1997) / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Details of virus | Empty: NO / Enveloped: NO / Isolate: SPECIES / Type: VIRION |
Buffer solution | pH: 6 |
Buffer component | Conc.: 0.1 mol/L / Name: citrate |
Specimen | Conc.: 1.32 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid type: Quantifoil R2/2 |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Tecnai Polara / Image courtesy: FEI Company |
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Microscopy | Model: FEI POLARA 300 |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 800 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
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Processing
EM software | Name: PHENIX / Version: 1.21.2_5419 / Category: model refinement |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
Symmetry | Point symmetry: I (icosahedral) |
3D reconstruction | Resolution: 4.08 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 17316 / Algorithm: FOURIER SPACE / Symmetry type: POINT |
Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL |
Atomic model building | PDB-ID: 6rtk![]() 6rtk Accession code: 6rtk / Source name: PDB / Type: experimental model |
Refinement | Cross valid method: NONE |