7ZUF
Saccharomyces cerevisiae L-BC virus, open particle, C5 reconstruction
This is a non-PDB format compatible entry.
Summary for 7ZUF
| Entry DOI | 10.2210/pdb7zuf/pdb |
| EMDB information | 14975 |
| Descriptor | Major capsid protein (1 entity in total) |
| Functional Keywords | open particle, totivirus, c5 asymmetric unit, virus |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 22 |
| Total formula weight | 1724663.86 |
| Authors | Grybchuk, D.,Prochazkova, M.,Fuzik, T.,Konovalovas, A.,Serva, S.,Yurchenko, V.,Plevka, P. (deposition date: 2022-05-12, release date: 2022-09-07, Last modification date: 2024-07-24) |
| Primary citation | Grybchuk, D.,Prochazkova, M.,Fuzik, T.,Konovalovas, A.,Serva, S.,Yurchenko, V.,Plevka, P. Structures of L-BC virus and its open particle provide insight into Totivirus capsid assembly. Commun Biol, 5:847-847, 2022 Cited by PubMed Abstract: L-BC virus persists in the budding yeast Saccharomyces cerevisiae, whereas other viruses from the family Totiviridae infect a diverse group of organisms including protists, fungi, arthropods, and vertebrates. The presence of totiviruses alters the fitness of the host organisms, for example, by maintaining the killer system in yeast or increasing the virulence of Leishmania guyanensis. Despite the importance of totiviruses for their host survival, there is limited information about Totivirus structure and assembly. Here we used cryo-electron microscopy to determine the structure of L-BC virus to a resolution of 2.9 Å. The L-BC capsid is organized with icosahedral symmetry, with each asymmetric unit composed of two copies of the capsid protein. Decamers of capsid proteins are stabilized by domain swapping of the C-termini of subunits located around icosahedral fivefold axes. We show that capsids of 9% of particles in a purified L-BC sample were open and lacked one decamer of capsid proteins. The existence of the open particles together with domain swapping within a decamer provides evidence that Totiviridae capsids assemble from the decamers of capsid proteins. Furthermore, the open particles may be assembly intermediates that are prepared for the incorporation of the virus (+) strand RNA. PubMed: 35986212DOI: 10.1038/s42003-022-03793-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (10 Å) |
Structure validation
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