4WLW

CRYSTAL STRUCTURE OF THE AG(I) (ACTIVATOR) FORM OF E. COLI CUER, A COPPER EFFLUX REGULATOR, BOUND TO COPA PROMOTER DNA

4WLW の概要

• エントリーDOI: 10.2210/pdb4wlw/pdb
• 関連するPDBエントリー: 4WLS
• 分子名称: HTH-type transcriptional regulator CueR, DNA NON-TEMPLATE STRAND (5-D(*DGP*DAP*DCP*DCP *DTP*DTP*DCP*DCP*DCP*DCP*DTP*DTP*DGP*DCP*DTP*DGP*DGP*DAP *DAP*DGP*DGP*DTP*DC)-3, DNA TEMPLATE STRAND (5-D(*DGP*DAP*DCP*DCP*DTP *DTP*DCP*DCP*DAP*DGP*DCP*DAP*DAP*DGP*DGP*DGP*DGP*DAP*DAP *DGP*DGP*DTP*DC)-3, ... (4 entities in total)
• 機能のキーワード: protein-dna complex, merr-family transcription regulator, ag(i)form, activator, transcription, transcription-dna complex, transcription/dna
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 29628.83

構造登録者

Philips, S.J.,Canalizo-Hernandez, M.,Mondragon, A.,O'Halloran, T.V. (登録日: 2014-10-08, 公開日: 2015-09-02, 最終更新日: 2024-10-16)

主引用文献

Philips, S.J.,Canalizo-Hernandez, M.,Yildirim, I.,Schatz, G.C.,Mondragon, A.,O'Halloran, T.V.
TRANSCRIPTION. Allosteric transcriptional regulation via changes in the overall topology of the core promoter.
Science, 349:877-881, 2015

PubMed Abstract: Many transcriptional activators act at a distance from core promoter elements and work by recruiting RNA polymerase through protein-protein interactions. We show here how the prokaryotic regulatory protein CueR both represses and activates transcription by differentially modulating local DNA structure within the promoter. Structural studies reveal that the repressor state slightly bends the promoter DNA, precluding optimal RNA polymerase-promoter recognition. Upon binding a metal ion in the allosteric site, CueR switches into an activator conformation. It maintains all protein-DNA contacts but introduces torsional stresses that kink and undertwist the promoter, stabilizing an A-form DNA-like conformation. These factors switch on and off transcription by exerting dynamic control of DNA stereochemistry, reshaping the core promoter and making it a better or worse substrate for polymerase.

PubMed: 26293965
DOI: 10.1126/science.aaa9809

実験手法

X-RAY DIFFRACTION (2.8 Å)