Summary for 9FKB
| Entry DOI | 10.2210/pdb9fkb/pdb |
| EMDB information | 50521 |
| Descriptor | HK97 gp6-like/SPP1 gp15-like head-tail connector, SPP1 gp17-like tail completion protein, Tail tube protein, ... (5 entities in total) |
| Functional Keywords | archeal virus, portal, tail, virus |
| Biological source | Haloferax tailed virus 1 More |
| Total number of polymer chains | 87 |
| Total formula weight | 1517065.11 |
| Authors | Zhang, D.,Daum, B.,Isupov, M.N.,McLaren, M. (deposition date: 2024-06-03, release date: 2025-06-18, Last modification date: 2025-10-22) |
| Primary citation | 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 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: 41042861DOI: 10.1126/sciadv.adx1178 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.96 Å) |
Structure validation
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