8RMP

Influenza polymerase A/H7N9-4M (ENDO(R) | Core1)

8RMP の概要

• エントリーDOI: 10.2210/pdb8rmp/pdb
• EMDBエントリー: 19366
• 分子名称: Polymerase acidic protein, RNA-directed RNA polymerase catalytic subunit, Polymerase basic protein 2, ... (4 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: 3
• 化学式量合計: 258315.49

構造登録者

Arragain, B.,Cusack, S. (登録日: 2024-01-08, 公開日: 2024-09-11)

主引用文献

Arragain, B.,Krischuns, T.,Pelosse, M.,Drncova, P.,Blackledge, M.,Naffakh, N.,Cusack, S.
Structures of influenza A and B replication complexes give insight into avian to human host adaptation and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase.
Nat Commun, 15:6910-6910, 2024

PubMed Abstract: Replication of influenza viral RNA depends on at least two viral polymerases, a parental replicase and an encapsidase, and cellular factor ANP32. ANP32 comprises an LRR domain and a long C-terminal low complexity acidic region (LCAR). Here we present evidence suggesting that ANP32 is recruited to the replication complex as an electrostatic chaperone that stabilises the encapsidase moiety within apo-polymerase symmetric dimers that are distinct for influenza A and B polymerases. The ANP32 bound encapsidase, then forms the asymmetric replication complex with the replicase, which is embedded in a parental ribonucleoprotein particle (RNP). Cryo-EM structures reveal the architecture of the influenza A and B replication complexes and the likely trajectory of the nascent RNA product into the encapsidase. The cryo-EM map of the FluB replication complex shows extra density attributable to the ANP32 LCAR wrapping around and stabilising the apo-encapsidase conformation. These structures give new insight into the various mutations that adapt avian strain polymerases to use the distinct ANP32 in mammalian cells.

PubMed: 39160148
DOI: 10.1038/s41467-024-51007-3

実験手法

ELECTRON MICROSCOPY (2.77 Å)