7AOF

Atomic structure of the poxvirus transcription late pre-initiation complex

7AOF の概要

• エントリーDOI: 10.2210/pdb7aof/pdb
• EMDBエントリー: 11843
• 分子名称: DNA-directed RNA polymerase 147 kDa polypeptide, MAGNESIUM ION, ZINC ION, ... (11 entities in total)
• 機能のキーワード: vaccinia, virus, rna polymerase, dna-dependent, pre-initiation complex, pic, initially melted, poxvirus, poxviridae, transcription
• 由来する生物種: Vaccinia virus GLV-1h68; 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 505583.84

構造登録者

Grimm, C.,Bartuli, J.,Fischer, U. (登録日: 2020-10-14, 公開日: 2021-10-06, 最終更新日: 2024-10-16)

主引用文献

Grimm, C.,Bartuli, J.,Boettcher, B.,Szalay, A.A.,Fischer, U.
Structural basis of the complete poxvirus transcription initiation process.
Nat.Struct.Mol.Biol., 28:779-788, 2021

PubMed Abstract: Poxviruses express their genes in the cytoplasm of infected cells using a virus-encoded multi-subunit polymerase (vRNAP) and unique transcription factors. We present cryo-EM structures that uncover the complete transcription initiation phase of the poxvirus vaccinia. In the pre-initiation complex, the heterodimeric early transcription factor VETFs/l adopts an arc-like shape spanning the polymerase cleft and anchoring upstream and downstream promoter elements. VETFI emerges as a TBP-like protein that inserts asymmetrically into the DNA major groove, triggers DNA melting, ensures promoter recognition and enforces transcription directionality. The helicase VETFs fosters promoter melting and the phospho-peptide domain (PPD) of vRNAP subunit Rpo30 enables transcription initiation. An unprecedented upstream promoter scrunching mechanism assisted by the helicase NPH-I probably fosters promoter escape and transition into elongation. Our structures shed light on unique mechanisms of poxviral gene expression and aid the understanding of thus far unexplained universal principles in transcription.

PubMed: 34556871
DOI: 10.1038/s41594-021-00655-w

実験手法

ELECTRON MICROSCOPY (2.98 Å)