8QPG

Turret of Haloferax tailed virus 1

これはPDB形式変換不可エントリーです。

8QPG の概要

• エントリーDOI: 10.2210/pdb8qpg/pdb
• EMDBエントリー: 18550
• 分子名称: Prokaryotic polysaccharide deacetylase, gp30, ZINC ION, ... (4 entities in total)
• 機能のキーワード: archeal virus, turret, turret capsid interface, mg ions, virus
• 由来する生物種: Haloferax tailed virus 1; 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 208467.26

構造登録者

Zhang, D.,Daum, B.,Isupov, M.N.,McLaren, M. (登録日: 2023-10-02, 公開日: 2024-10-09, 最終更新日: 2025-10-22)

主引用文献

Zhang, D.X.,Isupov, M.N.,Davies, R.M.,Schwarzer, S.,McLaren, M.,Stuart, W.S.,Gold, V.A.M.,Oksanen, H.M.,Quax, T.E.F.,Daum, B.
Cryo-EM resolves the structure of the archaeal dsDNA virus HFTV1 from head to tail.
Sci Adv, 11:eadx1178-eadx1178, 2025

PubMed Abstract: While archaeal viruses show a stunning diversity of morphologies, many bear a notable resemblance to tailed bacterial phages. This raises fundamental questions: Do all tailed viruses share a common origin and do they infect their hosts in similar ways? Answering these questions requires high-resolution structural insights, yet no complete atomic models of archaeal viruses have been available. Here, we present the near-atomic resolution structure of Haloferax tailed virus 1 (HFTV1), an archaeal virus thriving in extreme salinity. Using cryo-electron microscopy, we resolve the architecture and assembly of all structural proteins and capture conformational transitions associated with DNA ejection. Our data reveal genome spooling within the capsid and identify putative receptor-binding and catalytic sites for host recognition and infection. These findings uncover key mechanisms of archaeal virus assembly, principles of virus-host interactions, and evolutionary links connecting archaeal, bacterial, and eukaryotic viruses.

PubMed: 41042861
DOI: 10.1126/sciadv.adx1178

実験手法

ELECTRON MICROSCOPY (2.36 Å)