8PE4
Capsid structure of the L-A helper virus from native viral communities
Summary for 8PE4
| Entry DOI | 10.2210/pdb8pe4/pdb |
| Related | 8A5T |
| EMDB information | 15189 15214 15215 17628 |
| Descriptor | Major capsid protein (1 entity in total) |
| Functional Keywords | capsid structure scvla, viral particle, wildtype, endogenous, virus |
| Biological source | Saccharomyces cerevisiae virus L-A (baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 152140.06 |
| Authors | Schmidt, L.,Tueting, C.,Stubbs, M.T.,Kastritis, P.L. (deposition date: 2023-06-13, release date: 2024-05-22) |
| Primary citation | Schmidt, L.,Tuting, C.,Kyrilis, F.L.,Hamdi, F.,Semchonok, D.A.,Hause, G.,Meister, A.,Ihling, C.,Stubbs, M.T.,Sinz, A.,Kastritis, P.L. Delineating organizational principles of the endogenous L-A virus by cryo-EM and computational analysis of native cell extracts. Commun Biol, 7:557-557, 2024 Cited by PubMed Abstract: The high abundance of most viruses in infected host cells benefits their structural characterization. However, endogenous viruses are present in low copy numbers and are therefore challenging to investigate. Here, we retrieve cell extracts enriched with an endogenous virus, the yeast L-A virus. The determined cryo-EM structure discloses capsid-stabilizing cation-π stacking, widespread across viruses and within the Totiviridae, and an interplay of non-covalent interactions from ten distinct capsomere interfaces. The capsid-embedded mRNA decapping active site trench is supported by a constricting movement of two flexible opposite-facing loops. tRNA-loaded polysomes and other biomacromolecules, presumably mRNA, are found in virus proximity within the cell extract. Mature viruses participate in larger viral communities resembling their rare in-cell equivalents in terms of size, composition, and inter-virus distances. Our results collectively describe a 3D-architecture of a viral milieu, opening the door to cell-extract-based high-resolution structural virology. PubMed: 38730276DOI: 10.1038/s42003-024-06204-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.21 Å) |
Structure validation
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