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8PZQ

Model for focused reconstruction of influenza A RNP-like particle

8PZQ の概要
エントリーDOI10.2210/pdb8pzq/pdb
関連するPDBエントリー8PZP
EMDBエントリー18043 18044
分子名称Nucleoprotein, RNA (5'P-(UC)6-FAM3') (2 entities in total)
機能のキーワードinfluenza virus, nucleocapsid-like, rna binding protein., viral protein
由来する生物種Influenza A virus
詳細
タンパク質・核酸の鎖数5
化学式量合計179824.15
構造登録者
主引用文献Chenavier, F.,Estrozi, L.F.,Teulon, J.M.,Zarkadas, E.,Freslon, L.L.,Pellequer, J.L.,Ruigrok, R.W.H.,Schoehn, G.,Ballandras-Colas, A.,Crepin, T.
Cryo-EM structure of influenza helical nucleocapsid reveals NP-NP and NP-RNA interactions as a model for the genome encapsidation.
Sci Adv, 9:eadj9974-eadj9974, 2023
Cited by
PubMed Abstract: Influenza virus genome encapsidation is essential for the formation of a helical viral ribonucleoprotein (vRNP) complex composed of nucleoproteins (NP), the trimeric polymerase, and the viral genome. Although low-resolution vRNP structures are available, it remains unclear how the viral RNA is encapsidated and how NPs assemble into the helical filament specific of influenza vRNPs. In this study, we established a biological tool, the RNP-like particles assembled from recombinant influenza A virus NP and synthetic RNA, and we present the first subnanometric cryo-electron microscopy structure of the helical NP-RNA complex (8.7 to 5.3 Å). The helical RNP-like structure reveals a parallel double-stranded conformation, allowing the visualization of NP-NP and NP-RNA interactions. The RNA, located at the interface of neighboring NP protomers, interacts with conserved residues previously described as essential for the NP-RNA interaction. The NP undergoes conformational changes to enable RNA binding and helix formation. Together, our findings provide relevant insights for understanding the mechanism for influenza genome encapsidation.
PubMed: 38100595
DOI: 10.1126/sciadv.adj9974
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (5.3 Å)
構造検証レポート
Validation report summary of 8pzq
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-11に公開中

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