6EHM

Model of the Ebola virus nucleocapsid subunit from recombinant virus-like particles

6EHM の概要

• エントリーDOI: 10.2210/pdb6ehm/pdb
• EMDBエントリー: 3871
• 分子名称: Nucleoprotein, Membrane-associated protein VP24 (2 entities in total)
• 機能のキーワード: nucleocapsid, virus-like particle, virus like particle
• 由来する生物種: Zaire ebolavirus (strain Mayinga-76) (ZEBOV); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 223276.62

構造登録者

Wan, W.,Kolesnikova, L.,Clarke, M.,Koehler, A.,Noda, T.,Becker, S.,Briggs, J.A.G. (登録日: 2017-09-13, 公開日: 2017-11-08, 最終更新日: 2024-05-22)

主引用文献

Wan, W.,Kolesnikova, L.,Clarke, M.,Koehler, A.,Noda, T.,Becker, S.,Briggs, J.A.G.
Structure and assembly of the Ebola virus nucleocapsid.
Nature, 551:394-397, 2017

PubMed Abstract: Ebola and Marburg viruses are filoviruses: filamentous, enveloped viruses that cause haemorrhagic fever. Filoviruses are within the order Mononegavirales, which also includes rabies virus, measles virus, and respiratory syncytial virus. Mononegaviruses have non-segmented, single-stranded negative-sense RNA genomes that are encapsidated by nucleoprotein and other viral proteins to form a helical nucleocapsid. The nucleocapsid acts as a scaffold for virus assembly and as a template for genome transcription and replication. Insights into nucleoprotein-nucleoprotein interactions have been derived from structural studies of oligomerized, RNA-encapsidating nucleoprotein, and cryo-electron microscopy of nucleocapsid or nucleocapsid-like structures. There have been no high-resolution reconstructions of complete mononegavirus nucleocapsids. Here we apply cryo-electron tomography and subtomogram averaging to determine the structure of Ebola virus nucleocapsid within intact viruses and recombinant nucleocapsid-like assemblies. These structures reveal the identity and arrangement of the nucleocapsid components, and suggest that the formation of an extended α-helix from the disordered carboxy-terminal region of nucleoprotein-core links nucleoprotein oligomerization, nucleocapsid condensation, RNA encapsidation, and accessory protein recruitment.

PubMed: 29144446
DOI: 10.1038/nature24490

実験手法

ELECTRON MICROSCOPY (7.3 Å)