6XFA

Cryo-EM structure of EBV BFLF1

6XFA の概要

• エントリーDOI: 10.2210/pdb6xfa/pdb
• EMDBエントリー: 22168
• 分子名称: Packaging protein UL32, ZINC ION (2 entities in total)
• 機能のキーワード: viral packaging, viral cleavage, viral protein
• 由来する生物種: Epstein-Barr virus (strain GD1) (HHV-4)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 538096.15

構造登録者

Didychuk, A.L.,Gates, S.N.,Martin, A.,Glaunsinger, B. (登録日: 2020-06-15, 公開日: 2021-02-24, 最終更新日: 2024-03-06)

主引用文献

Didychuk, A.L.,Gates, S.N.,Gardner, M.R.,Strong, L.M.,Martin, A.,Glaunsinger, B.A.
A pentameric protein ring with novel architecture is required for herpesviral packaging.
Elife, 10:-, 2021

PubMed Abstract: Genome packaging in large double-stranded DNA viruses requires a powerful molecular motor to force the viral genome into nascent capsids, which involves essential accessory factors that are poorly understood. Here, we present structures of two such accessory factors from the oncogenic herpesviruses Kaposi's sarcoma-associated herpesvirus (KSHV; ORF68) and Epstein-Barr virus (EBV; BFLF1). These homologous proteins form highly similar homopentameric rings with a positively charged central channel that binds double-stranded DNA. Mutation of individual positively charged residues within but not outside the channel ablates DNA binding, and in the context of KSHV infection, these mutants fail to package the viral genome or produce progeny virions. Thus, we propose a model in which ORF68 facilitates the transfer of newly replicated viral genomes to the packaging motor.

PubMed: 33554858
DOI: 10.7554/eLife.62261

実験手法

ELECTRON MICROSCOPY (3.6 Å)