5DD8

The Crystal structure of HucR mutant (HucR-E48Q) from Deinococcus radiodurans

5DD8 の概要

• エントリーDOI: 10.2210/pdb5dd8/pdb
• 分子名称: Transcriptional regulator, MarR family, CHLORIDE ION (3 entities in total)
• 機能のキーワード: hucr, transcription factor, marr, transcription regulator
• 由来する生物種: Deinococcus radiodurans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39614.83

構造登録者

Deochand, D.K.,Perera, I.C.,Crochet, R.B.,Gilbert, N.C.,Newcomer, M.E.,Grove, A. (登録日: 2015-08-24, 公開日: 2015-09-09, 最終更新日: 2023-09-27)

主引用文献

Deochand, D.K.,Perera, I.C.,Crochet, R.B.,Gilbert, N.C.,Newcomer, M.E.,Grove, A.
Histidine switch controlling pH-dependent protein folding and DNA binding in a transcription factor at the core of synthetic network devices.
Mol Biosyst, 12:2417-2426, 2016

PubMed Abstract: Therapeutic strategies have been reported that depend on synthetic network devices in which a urate-sensing transcriptional regulator detects pathological levels of urate and triggers production or release of urate oxidase. The transcription factor involved, HucR, is a member of the multiple antibiotic resistance (MarR) protein family. We show that protonation of stacked histidine residues at the pivot point of long helices that form the scaffold of the dimer interface leads to reversible formation of a molten globule state and significantly attenuated DNA binding at physiological temperatures. We also show that binding of urate to symmetrical sites in each protein lobe is communicated via the dimer interface. This is the first demonstration of regulation of a MarR family transcription factor by pH-dependent interconversion between a molten globule and a compact folded state. Our data further suggest that HucR may be utilized in synthetic devices that depend on detection of pH changes.

PubMed: 27282811
DOI: 10.1039/c6mb00304d

実験手法

X-RAY DIFFRACTION (2.05 Å)