6RID

Structure of Vaccinia Virus DNA-dependent RNA polymerase elongation complex

6RID の概要

• エントリーDOI: 10.2210/pdb6rid/pdb
• 関連するPDBエントリー: 6RFG 6RFL 6RIE
• EMDBエントリー: 4868 4888 4889 4890 4891
• 分子名称: DNA-dependent RNA polymerase subunit rpo147, Template strand DNA, RNA, ... (13 entities in total)
• 機能のキーワード: vaccinia, rna polymerase, transcription, gene expression, viral protein
• 由来する生物種: Vaccinia virus GLV-1h68; 詳細
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 450981.11

構造登録者

Hillen, H.S.,Bartuli, J.,Grimm, C.,Dienemann, C.,Bedenk, K.,Szalar, A.,Fischer, U.,Cramer, P. (登録日: 2019-04-23, 公開日: 2019-12-18, 最終更新日: 2025-12-17)

主引用文献

Hillen, H.S.,Bartuli, J.,Grimm, C.,Dienemann, C.,Bedenk, K.,Szalay, A.A.,Fischer, U.,Cramer, P.
Structural Basis of Poxvirus Transcription: Transcribing and Capping Vaccinia Complexes.
Cell, 179:1525-, 2019

PubMed Abstract: Poxviruses use virus-encoded multisubunit RNA polymerases (vRNAPs) and RNA-processing factors to generate mG-capped mRNAs in the host cytoplasm. In the accompanying paper, we report structures of core and complete vRNAP complexes of the prototypic Vaccinia poxvirus (Grimm et al., 2019; in this issue of Cell). Here, we present the cryo-electron microscopy (cryo-EM) structures of Vaccinia vRNAP in the form of a transcribing elongation complex and in the form of a co-transcriptional capping complex that contains the viral capping enzyme (CE). The trifunctional CE forms two mobile modules that bind the polymerase surface around the RNA exit tunnel. RNA extends from the vRNAP active site through this tunnel and into the active site of the CE triphosphatase. Structural comparisons suggest that growing RNA triggers large-scale rearrangements on the surface of the transcription machinery during the transition from transcription initiation to RNA capping and elongation. Our structures unravel the basis for synthesis and co-transcriptional modification of poxvirus RNA.

PubMed: 31835031
DOI: 10.1016/j.cell.2019.11.023

実験手法

ELECTRON MICROSCOPY (2.9 Å)