6LDI

The cryo-EM structure of E. coli CueR transcription activation complex

6LDI の概要

• エントリーDOI: 10.2210/pdb6ldi/pdb
• EMDBエントリー: 0874
• 分子名称: DNA-directed RNA polymerase subunit alpha, ZINC ION, MAGNESIUM ION, ... (12 entities in total)
• 機能のキーワード: rna polymerase, cuer, transcription activation, transcription, transcription (dna to rna)
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 527205.42

構造登録者

Fang, C.L.,Zhang, Y. (登録日: 2019-11-21, 公開日: 2020-09-30, 最終更新日: 2024-03-27)

主引用文献

Fang, C.,Philips, S.J.,Wu, X.,Chen, K.,Shi, J.,Shen, L.,Xu, J.,Feng, Y.,O'Halloran, T.V.,Zhang, Y.
CueR activates transcription through a DNA distortion mechanism.
Nat.Chem.Biol., 17:57-64, 2021

PubMed Abstract: The MerR-family transcription factors (TFs) are a large group of bacterial proteins responding to cellular metal ions and multiple antibiotics by binding within central RNA polymerase-binding regions of a promoter. While most TFs alter transcription through protein-protein interactions, MerR TFs are capable of reshaping promoter DNA. To address the question of which mechanism prevails, we determined two cryo-EM structures of transcription activation complexes (TAC) comprising Escherichia coli CueR (a prototype MerR TF), RNAP holoenzyme and promoter DNA. The structures reveal that this TF promotes productive promoter-polymerase association without canonical protein-protein contacts seen between other activator proteins and RNAP. Instead, CueR realigns the key promoter elements in the transcription activation complex by clamp-like protein-DNA interactions: these induce four distinct kinks that ultimately position the -10 element for formation of the transcription bubble. These structural and biochemical results provide strong support for the DNA distortion paradigm of allosteric transcriptional control by MerR TFs.

PubMed: 32989300
DOI: 10.1038/s41589-020-00653-x

実験手法

ELECTRON MICROSCOPY (3.69 Å)