6SCO
Cryo-EM Structure of Potato Leaf Roll Virus VLP
Summary for 6SCO
| Entry DOI | 10.2210/pdb6sco/pdb |
| EMDB information | 10142 10144 |
| Descriptor | Coat protein (1 entity in total) |
| Functional Keywords | luteovirus, polerovirus, vlp, capsid., virus like particle |
| Biological source | Potato leafroll virus (PLrV) |
| Total number of polymer chains | 3 |
| Total formula weight | 69580.17 |
| Authors | Byrne, M.J.,Ranson, N.A. (deposition date: 2019-07-25, release date: 2019-10-02, Last modification date: 2024-05-22) |
| Primary citation | Byrne, M.J.,Steele, J.F.C.,Hesketh, E.L.,Walden, M.,Thompson, R.F.,Lomonossoff, G.P.,Ranson, N.A. Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles. Structure, 27:1761-, 2019 Cited by PubMed Abstract: The Luteoviridae are pathogenic plant viruses responsible for significant crop losses worldwide. They infect a wide range of food crops, including cereals, legumes, cucurbits, sugar beet, sugarcane, and potato and, as such, are a major threat to global food security. Viral replication is strictly limited to the plant vasculature, and this phloem limitation, coupled with the need for aphid transmission of virus particles, has made it difficult to generate virus in the quantities needed for high-resolution structural studies. Here, we exploit recent advances in heterologous expression in plants to produce sufficient quantities of virus-like particles for structural studies. We have determined their structures to high resolution by cryoelectron microscopy, providing the molecular-level insight required to rationally interrogate luteovirid capsid formation and aphid transmission, thereby providing a platform for the development of preventive agrochemicals for this important family of plant viruses. PubMed: 31611039DOI: 10.1016/j.str.2019.09.010 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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