6RVS

Atomic structure of the Epstein-Barr portal, structure II

Summary for 6RVS

• Entry DOI: 10.2210/pdb6rvs/pdb
• EMDB information: 10011
• Descriptor: Portal protein (1 entity in total)
• Functional Keywords: viral protein, dna packaging protein
• Biological source: Epstein-Barr virus (strain GD1) (HHV-4)
• Total number of polymer chains: 12
• Total formula weight: 822475.69

Authors

Machon, C.,Fabrega-Ferrer, M.,Zhou, D.,Cuervo, A.,Carrascosa, J.L.,Stuart, D.I.,Coll, M. (deposition date: 2019-05-31, release date: 2019-09-18, Last modification date: 2024-05-22)

Primary citation

Machon, C.,Fabrega-Ferrer, M.,Zhou, D.,Cuervo, A.,Carrascosa, J.L.,Stuart, D.I.,Coll, M.
Atomic structure of the Epstein-Barr virus portal.
Nat Commun, 10:3891-3891, 2019

PubMed Abstract: Herpesviridae is a vast family of enveloped DNA viruses that includes eight distinct human pathogens, responsible for diseases that range from almost asymptomatic to severe and life-threatening. Epstein-Barr virus infects B-cells and epithelial cells, causing infectious mononucleosis, as well as a number of cancers. Epstein-Barr infection cannot be cured since neither vaccine nor antiviral drug treatments are available. All herpesviruses contain a linear double-stranded DNA genome, enclosed within an icosahedral capsid. Viral portal protein plays a key role in the procapsid assembly and DNA packaging. The portal is the entrance and exit pore for the viral genome, making it an attractive pharmacological target for the development of new antivirals. Here we present the atomic structure of the portal protein of Epstein-Barr virus, solved by cryo-electron microscopy at 3.5 Å resolution. The detailed architecture of this protein suggests that it plays a functional role in DNA retention during packaging.

PubMed: 31467275
DOI: 10.1038/s41467-019-11706-8

Experimental method

ELECTRON MICROSCOPY (3.59 Å)