7BSI

Epstein-Barr virus, one asymmetric unit structure of the icosahedral tegumented capsid

これはPDB形式変換不可エントリーです。

7BSI の概要

• エントリーDOI: 10.2210/pdb7bsi/pdb
• EMDBエントリー: 30162
• 分子名称: Small capsomere-interacting protein, Major capsid protein, Triplex capsid protein 1, ... (4 entities in total)
• 機能のキーワード: tegumented capsid, icosahedral reconstruction, virus
• 由来する生物種: Epstein-Barr virus (strain B95-8) (HHV-4); 詳細
• タンパク質・核酸の鎖数: 47
• 化学式量合計: 3288792.93

構造登録者

Li, Z.,Yu, X. (登録日: 2020-03-30, 公開日: 2020-09-30, 最終更新日: 2024-10-16)

主引用文献

Li, Z.,Zhang, X.,Dong, L.,Pang, J.,Xu, M.,Zhong, Q.,Zeng, M.S.,Yu, X.
CryoEM structure of the tegumented capsid of Epstein-Barr virus.
Cell Res., 30:873-884, 2020

PubMed Abstract: Epstein-Barr virus (EBV) is the primary cause of infectious mononucleosis and has been shown to be closely associated with various malignancies. Here, we present a complete atomic model of EBV, including the icosahedral capsid, the dodecameric portal and the capsid-associated tegument complex (CATC). Our in situ portal from the tegumented capsid adopts a closed conformation with its channel valve holding the terminal viral DNA and with its crown region firmly engaged by three layers of ring-like dsDNA, which, together with the penton flexibility, effectively alleviates the capsid inner pressure placed on the portal cap. In contrast, the CATCs, through binding to the flexible penton vertices in a stoichiometric manner, accurately increase the inner capsid pressure to facilitate the pressure-driven genome delivery. Together, our results provide important insights into the mechanism by which the EBV capsid, portal, packaged genome and the CATCs coordinately achieve a pressure balance to simultaneously benefit both viral genome retention and ejection.

PubMed: 32620850
DOI: 10.1038/s41422-020-0363-0

実験手法

ELECTRON MICROSCOPY (4.1 Å)