7BQT
Epstein-Barr virus, C12 portal dodecamer
Summary for 7BQT
| Entry DOI | 10.2210/pdb7bqt/pdb |
| EMDB information | 30155 |
| Descriptor | Portal protein (1 entity in total) |
| Functional Keywords | epstein-barr virus, portal dodecomer, tegumented capsid, viral protein |
| Biological source | Epstein-Barr virus (strain B95-8) (HHV-4) |
| Total number of polymer chains | 12 |
| Total formula weight | 822475.69 |
| Authors | |
| Primary citation | 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 Cited by 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: 32620850DOI: 10.1038/s41422-020-0363-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.8 Å) |
Structure validation
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