7ADC

Transcription termination intermediate complex 3 delta NusG

7ADC の概要

• エントリーDOI: 10.2210/pdb7adc/pdb
• EMDBエントリー: 11723
• 分子名称: Transcription termination factor Rho, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (14 entities in total)
• 機能のキーワード: rna polymerase, rho, transcription
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 15
• 化学式量合計: 793396.90

構造登録者

Said, N.,Hilal, T.,Loll, B.,Wahl, C.M. (登録日: 2020-09-14, 公開日: 2020-11-25, 最終更新日: 2025-04-09)

主引用文献

Said, N.,Hilal, T.,Sunday, N.D.,Khatri, A.,Burger, J.,Mielke, T.,Belogurov, G.A.,Loll, B.,Sen, R.,Artsimovitch, I.,Wahl, M.C.
Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase rho.
Science, 371:-, 2021

PubMed Abstract: Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) ρ on a pathway to terminating NusA/NusG-modified elongation complexes. An open ρ ring contacts NusA, NusG, and multiple regions of RNA polymerase, trapping and locally unwinding proximal upstream DNA. NusA wedges into the ρ ring, initially sequestering RNA. Upon deflection of distal upstream DNA over the RNA polymerase zinc-binding domain, NusA rotates underneath one capping ρ subunit, which subsequently captures RNA. After detachment of NusG and clamp opening, RNA polymerase loses its grip on the RNA:DNA hybrid and is inactivated. Our structural and functional analyses suggest that ρ, and other termination factors across life, may use analogous strategies to allosterically trap transcription complexes in a moribund state.

PubMed: 33243850
DOI: 10.1126/science.abd1673

実験手法

ELECTRON MICROSCOPY (4 Å)