7QWZ

Full capsid of Saccharomyces cerevisiae virus L-BCLa

Summary for 7QWZ

• Entry DOI: 10.2210/pdb7qwz/pdb
• EMDB information: 14195
• Descriptor: Major capsid protein (1 entity in total)
• Functional Keywords: capsid protein dimer, icosahedral asymmetric unit, totivirus capsid, virus
• Biological source: Saccharomyces cerevisiae virus L-BC (La)
• Total number of polymer chains: 2
• Total formula weight: 156787.62

Authors

Grybchuk, D.,Prochazkova, M.,Fuzik, T.,Konovalovas, A.,Serva, S.,Yurchenko, V.,Plevka, P. (deposition date: 2022-01-26, release date: 2022-09-07, Last modification date: 2024-07-17)

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

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: 35986212
DOI: 10.1038/s42003-022-03793-z

Experimental method

ELECTRON MICROSCOPY (3.7 Å)