8R3L

Influenza A/H7N9 polymerase in pre-initiation state, intermediate conformation (I) with PB2-C(I), ENDO(T), and Pol II pS5 CTD peptide mimic bound in site 1A/2A

8R3L の概要

• エントリーDOI: 10.2210/pdb8r3l/pdb
• EMDBエントリー: 18872
• 分子名称: Polymerase acidic protein, RNA-directed RNA polymerase catalytic subunit, Polymerase basic protein 2, ... (5 entities in total)
• 機能のキーワード: viral polymerase, viral protein
• 由来する生物種: Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9)); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 296738.89

構造登録者

Arragain, B.,Cusack, S. (登録日: 2023-11-09, 公開日: 2024-02-21, 最終更新日: 2025-07-02)

主引用文献

Krischuns, T.,Arragain, B.,Isel, C.,Paisant, S.,Budt, M.,Wolff, T.,Cusack, S.,Naffakh, N.
The host RNA polymerase II C-terminal domain is the anchor for replication of the influenza virus genome.
Nat Commun, 15:1064-1064, 2024

PubMed Abstract: The current model is that the influenza virus polymerase (FluPol) binds either to host RNA polymerase II (RNAP II) or to the acidic nuclear phosphoprotein 32 (ANP32), which drives its conformation and activity towards transcription or replication of the viral genome, respectively. Here, we provide evidence that the FluPol-RNAP II binding interface, beyond its well-acknowledged function in cap-snatching during transcription initiation, has also a pivotal role in replication of the viral genome. Using a combination of cell-based and in vitro approaches, we show that the RNAP II C-terminal-domain, jointly with ANP32, enhances FluPol replication activity. We observe successive conformational changes to switch from a transcriptase to a replicase conformation in the presence of the bound RNPAII C-terminal domain and propose a model in which the host RNAP II is the anchor for transcription and replication of the viral genome. Our data open new perspectives on the spatial coupling of viral transcription and replication and the coordinated balance between these two activities.

PubMed: 38316757
DOI: 10.1038/s41467-024-45205-2

実験手法

ELECTRON MICROSCOPY (3.25 Å)