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8A5T

Capsid structure of the L-A helper virus from native viral communities

Summary for 8A5T
Entry DOI10.2210/pdb8a5t/pdb
EMDB information15189
DescriptorMajor capsid protein (1 entity in total)
Functional Keywordscapsid structure scvla, viral particle, wildtype, endogenous, virus
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Total number of polymer chains2
Total formula weight152140.06
Authors
Schmidt, L.,Tueting, C.,Stubbs, M.T.,Kastritis, P.L. (deposition date: 2022-06-16, release date: 2023-12-20, Last modification date: 2024-05-22)
Primary citationSchmidt, 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: 38730276
DOI: 10.1038/s42003-024-06204-7
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.78 Å)
Structure validation

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数据于2025-06-25公开中

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