7EXA

Structure of mumps virus nucleoprotein without C-arm

7EXA の概要

• エントリーDOI: 10.2210/pdb7exa/pdb
• EMDBエントリー: 31367
• 分子名称: Nucleoprotein, RNA (5'-R(P*UP*UP*UP*UP*UP*U)-3') (2 entities in total)
• 機能のキーワード: nucleocapsid, mumps virus, nuclear protein
• 由来する生物種: Mumps virus (strain Jeryl-Lynn) (MuV); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63262.04

構造登録者

Shen, Q.,Shan, H.,Zhang, N.,Qin, Y. (登録日: 2021-05-26, 公開日: 2024-08-21)

主引用文献

Shan, H.,Su, X.,Li, T.,Qin, Y.,Zhang, N.,Yang, L.,Ma, L.,Bai, Y.,Qi, L.,Liu, Y.,Shen, Q.T.
Structural plasticity of mumps virus nucleocapsids with cryo-EM structures.
Commun Biol, 4:833-833, 2021

PubMed Abstract: Mumps virus (MuV) is a highly contagious human pathogen and frequently causes worldwide outbreaks despite available vaccines. Similar to other mononegaviruses such as Ebola and rabies, MuV uses a single-stranded negative-sense RNA as its genome, which is enwrapped by viral nucleoproteins into the helical nucleocapsid. The nucleocapsid acts as a scaffold for genome condensation and as a template for RNA replication and transcription. Conformational changes in the MuV nucleocapsid are required to switch between different activities, but the underlying mechanism remains elusive due to the absence of high-resolution structures. Here, we report two MuV nucleoprotein-RNA rings with 13 and 14 protomers, one stacked-ring filament and two nucleocapsids with distinct helical pitches, in dense and hyperdense states, at near-atomic resolutions using cryo-electron microscopy. Structural analysis of these in vitro assemblies indicates that the C-terminal tail of MuV nucleoprotein likely regulates the assembly of helical nucleocapsids, and the C-terminal arm may be relevant for the transition between the dense and hyperdense states of helical nucleocapsids. Our results provide the molecular mechanism for structural plasticity among different MuV nucleocapsids and create a possible link between structural plasticity and genome condensation.

PubMed: 34215847
DOI: 10.1038/s42003-021-02362-0

実験手法

ELECTRON MICROSCOPY (2.9 Å)