6T0V

Bat Influenza A polymerase elongation complex with incoming UTP analogue (complete polymerase)

6T0V の概要

• エントリーDOI: 10.2210/pdb6t0v/pdb
• EMDBエントリー: 10360
• 分子名称: Polymerase acidic protein, RNA-directed RNA polymerase catalytic subunit, Polymerase basic protein 2, ... (9 entities in total)
• 機能のキーワード: influenza, polymerase, viral transcription, rna, viral protein
• 由来する生物種: Influenza A virus (A/little yellow-shouldered bat/Guatemala/060/2010(H17N10)); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 285414.46

構造登録者

Wandzik, J.M.,Kouba, T.,Cusack, S. (登録日: 2019-10-03, 公開日: 2020-04-15, 最終更新日: 2024-05-22)

主引用文献

Wandzik, J.M.,Kouba, T.,Karuppasamy, M.,Pflug, A.,Drncova, P.,Provaznik, J.,Azevedo, N.,Cusack, S.
A Structure-Based Model for the Complete Transcription Cycle of Influenza Polymerase.
Cell, 181:877-, 2020

PubMed Abstract: Influenza polymerase uses unique mechanisms to synthesize capped and polyadenylated mRNAs from the genomic viral RNA (vRNA) template, which is packaged inside ribonucleoprotein particles (vRNPs). Here, we visualize by cryoelectron microscopy the conformational dynamics of the polymerase during the complete transcription cycle from pre-initiation to termination, focusing on the template trajectory. After exiting the active site cavity, the template 3' extremity rebinds into a specific site on the polymerase surface. Here, it remains sequestered during all subsequent transcription steps, forcing the template to loop out as it further translocates. At termination, the strained connection between the bound template 5' end and the active site results in polyadenylation by stuttering at uridine 17. Upon product dissociation, further conformational changes release the trapped template, allowing recycling back into the pre-initiation state. Influenza polymerase thus performs transcription while tightly binding to and protecting both template ends, allowing efficient production of multiple mRNAs from a single vRNP.

PubMed: 32304664
DOI: 10.1016/j.cell.2020.03.061

実験手法

ELECTRON MICROSCOPY (3.02 Å)