6QCT

Influenza B polymerase elongation complex

6QCT の概要

• エントリーDOI: 10.2210/pdb6qct/pdb
• EMDBエントリー: 4511 4512
• 分子名称: Polymerase acidic protein, RNA-directed RNA polymerase catalytic subunit, Polymerase basic protein 2, ... (7 entities in total)
• 機能のキーワード: influenza b polymerase, viral protein
• 由来する生物種: Influenza B virus (B/Memphis/13/2003); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 280925.33

構造登録者

Cusack, S.,Kouba, T. (登録日: 2018-12-30, 公開日: 2019-06-05, 最終更新日: 2025-07-02)

主引用文献

Kouba, T.,Drncova, P.,Cusack, S.
Structural snapshots of actively transcribing influenza polymerase.
Nat.Struct.Mol.Biol., 26:460-470, 2019

PubMed Abstract: Influenza virus RNA-dependent RNA polymerase uses unique mechanisms to transcribe its single-stranded genomic viral RNA (vRNA) into messenger RNA. The polymerase is initially bound to a promoter comprising the partially base-paired 3' and 5' extremities of the RNA. A short, capped primer, 'cap-snatched' from a nascent host polymerase II transcript, is directed towards the polymerase active site to initiate RNA synthesis. Here we present structural snapshots, as determined by X-ray crystallography and cryo-electron microscopy, of actively initiating influenza polymerase as it transitions towards processive elongation. Unexpected conformational changes unblock the active site cavity to allow establishment of a nine-base-pair template-product RNA duplex before the strands separate into distinct exit channels. Concomitantly, as the template translocates, the promoter base pairs are broken and the template entry region is remodeled. These structures reveal details of the influenza polymerase active site that will help optimize nucleoside analogs or other compounds that directly inhibit viral RNA synthesis.

PubMed: 31160782
DOI: 10.1038/s41594-019-0232-z

実験手法

ELECTRON MICROSCOPY (3.2 Å)