7NT5

CryoEM structure of the Nipah virus nucleocapsid single helical turn assembly

7NT5 の概要

• エントリーDOI: 10.2210/pdb7nt5/pdb
• EMDBエントリー: 12581
• 分子名称: Nucleoprotein, RNA (78-MER) (2 entities in total)
• 機能のキーワード: protein-rna complex, nucleocapsid, viral protein
• 由来する生物種: Nipah virus; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 811759.28

構造登録者

Ker, D.S.,Jenkins, H.T.,Greive, S.J.,Antson, A.A. (登録日: 2021-03-09, 公開日: 2021-07-07, 最終更新日: 2024-07-10)

主引用文献

Ker, D.S.,Jenkins, H.T.,Greive, S.J.,Antson, A.A.
CryoEM structure of the Nipah virus nucleocapsid assembly.
Plos Pathog., 17:e1009740-e1009740, 2021

PubMed Abstract: Nipah and its close relative Hendra are highly pathogenic zoonotic viruses, storing their ssRNA genome in a helical nucleocapsid assembly formed by the N protein, a major viral immunogen. Here, we report the first cryoEM structure for a Henipavirus RNA-bound nucleocapsid assembly, at 3.5 Å resolution. The helical assembly is stabilised by previously undefined N- and C-terminal segments, contributing to subunit-subunit interactions. RNA is wrapped around the nucleocapsid protein assembly with a periodicity of six nucleotides per protomer, in the "3-bases-in, 3-bases-out" conformation, with protein plasticity enabling non-sequence specific interactions. The structure reveals commonalities in RNA binding pockets and in the conformation of bound RNA, not only with members of the Paramyxoviridae family, but also with the evolutionarily distant Filoviridae Ebola virus. Significant structural differences with other Paramyxoviridae members are also observed, particularly in the position and length of the exposed α-helix, residues 123-139, which may serve as a valuable epitope for surveillance and diagnostics.

PubMed: 34270629
DOI: 10.1371/journal.ppat.1009740

実験手法

ELECTRON MICROSCOPY (3.5 Å)