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8QSY

Portal capsid interface of full Haloferax tailed virus 1.

This is a non-PDB format compatible entry.
Summary for 8QSY
Entry DOI10.2210/pdb8qsy/pdb
Related8QQN
EMDB information18642
DescriptorHK97 gp5-like major capsid protein, Capsid stabilization protein, Hypothetical protein gp21, ... (7 entities in total)
Functional Keywordsarchaeal virus, portal, portal capsid interface, mg ions, virus
Biological sourceHaloferax tailed virus 1
More
Total number of polymer chains74
Total formula weight2664283.45
Authors
Zhang, D.,Daum, B.,Isupov, M.N.,McLaren, M. (deposition date: 2023-10-11, release date: 2024-10-23, Last modification date: 2025-10-22)
Primary citationZhang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.68 Å)
Structure validation

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