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9FHP

CryoEM structure of wild-type Turnip Yellows Virus

Summary for 9FHP
Entry DOI10.2210/pdb9fhp/pdb
Related6rtk
EMDB information10003
DescriptorMinor capsid readthrough protein (1 entity in total)
Functional Keywordsread-through protein, virus
Biological sourceTurnip yellows virus
Total number of polymer chains3
Total formula weight67567.56
Authors
Trapani, S.,Lai Kee Him, J.,Hoh, F.,Brault, V.,Bron, P. (deposition date: 2024-05-28, release date: 2024-06-05, Last modification date: 2025-05-21)
Primary citationLai-Kee-Him, J.,Trapani, S.,Boissinot, S.,Reinbold, C.,Fallet, C.,Ancelin, A.,Lecorre, F.,Hoh, F.,Ziegler-Graff, V.,Brault, V.,Bron, P.
Structure of the turnip yellows virus particles.
Virology, 607:110514-110514, 2025
Cited by
PubMed 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 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.
PubMed: 40179450
DOI: 10.1016/j.virol.2025.110514
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.08 Å)
Structure validation

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