6N57

Cryo-EM structure of Escherichia coli RNAP polymerase bound with TraR in conformation I

6N57 の概要

• エントリーDOI: 10.2210/pdb6n57/pdb
• EMDBエントリー: 0348 0349
• 分子名称: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (9 entities in total)
• 機能のキーワード: protein-dna complex, transcription initiation, rna polyermase, dna promoter melting, transcription, transferase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 473918.36

構造登録者

Chen, J.,Chiu, C.E.,Campbell, E.A.,Darst, S.A. (登録日: 2018-11-21, 公開日: 2020-02-26, 最終更新日: 2025-06-04)

主引用文献

Chen, J.,Gopalkrishnan, S.,Chiu, C.,Chen, A.Y.,Campbell, E.A.,Gourse, R.L.,Ross, W.,Darst, S.A.
E. coliTraR allosterically regulates transcription initiation by altering RNA polymerase conformation.
Elife, 8:-, 2019

PubMed Abstract: TraR and its homolog DksA are bacterial proteins that regulate transcription initiation by binding directly to RNA polymerase (RNAP) rather than to promoter DNA. Effects of TraR mimic the combined effects of DksA and its cofactor ppGpp, but the structural basis for regulation by these factors remains unclear. Here, we use cryo-electron microscopy to determine structures of RNAP, with or without TraR, and of an RNAP-promoter complex. TraR binding induced RNAP conformational changes not seen in previous crystallographic analyses, and a quantitative analysis revealed TraR-induced changes in RNAP conformational heterogeneity. These changes involve mobile regions of RNAP affecting promoter DNA interactions, including the βlobe, the clamp, the bridge helix, and several lineage-specific insertions. Using mutational approaches, we show that these structural changes, as well as effects on σ region 1.1, are critical for transcription activation or inhibition, depending on the kinetic features of regulated promoters.

PubMed: 31841111
DOI: 10.7554/eLife.49375

実験手法

ELECTRON MICROSCOPY (3.7 Å)