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6RFL

Structure of the complete Vaccinia DNA-dependent RNA polymerase complex

6RFL の概要
エントリーDOI10.2210/pdb6rfl/pdb
EMDBエントリー4868
分子名称DNA-dependent RNA polymerase subunit rpo132, Transcription factor VETF 82kDa large subunit, chr17.trna16-GlnTTG, ... (18 entities in total)
機能のキーワードvaccinia, rna polymerase, rna polymerase complex, rnap, vrnap, complete vrnap, 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16
化学式量合計843670.31
構造登録者
主引用文献Grimm, C.,Hillen, H.S.,Bedenk, K.,Bartuli, J.,Neyer, S.,Zhang, Q.,Huttenhofer, A.,Erlacher, M.,Dienemann, C.,Schlosser, A.,Urlaub, H.,Bottcher, B.,Szalay, A.A.,Cramer, P.,Fischer, U.
Structural Basis of Poxvirus Transcription: Vaccinia RNA Polymerase Complexes.
Cell, 179:1537-1550.e19, 2019
Cited by
PubMed Abstract: Poxviruses encode a multisubunit DNA-dependent RNA polymerase (vRNAP) that carries out viral gene expression in the host cytoplasm. We report cryo-EM structures of core and complete vRNAP enzymes from Vaccinia virus at 2.8 Å resolution. The vRNAP core enzyme resembles eukaryotic RNA polymerase II (Pol II) but also reveals many virus-specific features, including the transcription factor Rap94. The complete enzyme additionally contains the transcription factor VETF, the mRNA processing factors VTF/CE and NPH-I, the viral core protein E11, and host tRNA. This complex can carry out the entire early transcription cycle. The structures show that Rap94 partially resembles the Pol II initiation factor TFIIB, that the vRNAP subunit Rpo30 resembles the Pol II elongation factor TFIIS, and that NPH-I resembles chromatin remodeling enzymes. Together with the accompanying paper (Hillen et al., 2019), these results provide the basis for unraveling the mechanisms of poxvirus transcription and RNA processing.
PubMed: 31835032
DOI: 10.1016/j.cell.2019.11.024
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.76 Å)
構造検証レポート
Validation report summary of 6rfl
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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