8PE4

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

8PE4 の概要

• エントリーDOI: 10.2210/pdb8pe4/pdb
• 関連するPDBエントリー: 8A5T
• EMDBエントリー: 15189 15214 15215 17628
• 分子名称: Major capsid protein (1 entity in total)
• 機能のキーワード: capsid structure scvla, viral particle, wildtype, endogenous, virus
• 由来する生物種: Saccharomyces cerevisiae virus L-A (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 152140.06

構造登録者

Schmidt, L.,Tueting, C.,Stubbs, M.T.,Kastritis, P.L. (登録日: 2023-06-13, 公開日: 2024-05-22)

主引用文献

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

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

実験手法

ELECTRON MICROSCOPY (3.21 Å)