6I54

Influenza A nucleoprotein docked into 3D helical structure of the wild type ribonucleoprotein complex obtained using cryoEM. Conformation 2.

6I54 の概要

• エントリーDOI: 10.2210/pdb6i54/pdb
• EMDBエントリー: 0175 4412
• 分子名称: Nucleoprotein, Influenza virus nucleoprotein (2 entities in total)
• 機能のキーワード: influenza a virus ribonucleoprotein rna binding protein, viral protein
• 由来する生物種: Influenza A virus (A/Wilson-Smith/1933(H1N1)); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 90373.15

構造登録者

Coloma, R.,Arranz, R.,de la Rosa-Trevin, J.M.,Sorzano, C.O.S.,Carlero, D.,Ortin, J.,Martin-Benito, J. (登録日: 2018-11-12, 公開日: 2019-11-13, 最終更新日: 2024-05-15)

主引用文献

Coloma, R.,Arranz, R.,de la Rosa-Trevin, J.M.,Sorzano, C.O.S.,Munier, S.,Carlero, D.,Naffakh, N.,Ortin, J.,Martin-Benito, J.
Structural insights into influenza A virus ribonucleoproteins reveal a processive helical track as transcription mechanism.
Nat Microbiol, 5:727-734, 2020

PubMed Abstract: The influenza virus genome consists of eight viral ribonucleoproteins (vRNPs), each consisting of a copy of the polymerase, one of the genomic RNA segments and multiple copies of the nucleoprotein arranged in a double helical conformation. vRNPs are macromolecular machines responsible for messenger RNA synthesis and genome replication, that is, the formation of progeny vRNPs. Here, we describe the structural basis of the transcription process. The mechanism, which we call the 'processive helical track', is based on the extreme flexibility of the helical part of the vRNP that permits a sliding movement between both antiparallel nucleoprotein-RNA strands, thereby allowing the polymerase to move over the genome while bound to both RNA ends. Accordingly, we demonstrate that blocking this movement leads to inhibition of vRNP transcriptional activity. This mechanism also reveals a critical role of the nucleoprotein in maintaining the double helical structure throughout the copying process to make the RNA template accessible to the polymerase.

PubMed: 32152587
DOI: 10.1038/s41564-020-0675-3

実験手法

ELECTRON MICROSCOPY (10 Å)