6RFG

Structure of the Vaccinia core protein E11

6RFG の概要

• エントリーDOI: 10.2210/pdb6rfg/pdb
• 分子名称: 15 kDa core protein (2 entities in total)
• 機能のキーワード: e11, e11l, vaccinia, core protein, rna polymerase complex, viral protein
• 由来する生物種: Vaccinia virus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68313.74

構造登録者

Grimm, C.,Fischer, U. (登録日: 2019-04-15, 公開日: 2019-12-11, 最終更新日: 2024-05-15)

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

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

実験手法

X-RAY DIFFRACTION (1.897 Å)