8PEW

Rho-ATPgS-Psu complex III expanded

8PEW の概要

• エントリーDOI: 10.2210/pdb8pew/pdb
• 関連するPDBエントリー: 8PEU
• EMDBエントリー: 17637 17639
• 分子名称: Transcription termination factor Rho, Polarity suppression protein, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: transcription termination, phage inhibitor, gene regulation
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 34
• 化学式量合計: 1198312.88

構造登録者

Gjorgjevikj, D.,Wahl, M.C.,Hilal, T.,Loll, B. (登録日: 2023-06-15, 公開日: 2024-06-26, 最終更新日: 2025-01-22)

主引用文献

Gjorgjevikj, D.,Kumar, N.,Wang, B.,Hilal, T.,Said, N.,Loll, B.,Artsimovitch, I.,Sen, R.,Wahl, M.C.
The Psu protein of phage satellite P4 inhibits transcription termination factor rho by forced hyper-oligomerization.
Nat Commun, 16:550-550, 2025

PubMed Abstract: Many bacteriophages modulate host transcription to favor expression of their own genomes. Phage satellite P4 polarity suppression protein, Psu, a building block of the viral capsid, inhibits hexameric transcription termination factor, ρ, by presently unknown mechanisms. Our cryogenic electron microscopy structures of ρ-Psu complexes show that Psu dimers clamp two inactive, open ρ rings and promote their expansion to higher-oligomeric states. ATPase, nucleotide binding and nucleic acid binding studies revealed that Psu hinders ρ ring closure and traps nucleotides in their binding pockets on ρ. Structure-guided mutagenesis in combination with growth, pull-down, and termination assays further delineated the functional ρ-Psu interfaces in vivo. Bioinformatic analyses revealed that Psu is associated with a wide variety of phage defense systems across Enterobacteriaceae, suggesting that Psu may regulate expression of anti-phage genes. Our findings show that modulation of the ρ oligomeric state via diverse strategies is a pervasive gene regulatory principle in bacteria.

PubMed: 39788982
DOI: 10.1038/s41467-025-55897-9

実験手法

ELECTRON MICROSCOPY (4.3 Å)