5FRH

Solution structure of oxidised RsrA

5FRH の概要

• エントリーDOI: 10.2210/pdb5frh/pdb
• NMR情報: BMRB: 25956
• 分子名称: ANTI-SIGMA FACTOR RSRA (1 entity in total)
• 機能のキーワード: transcription, anti-sigma factor, streptomyces coelicolor, redox sensing
• 由来する生物種: STREPTOMYCES COELICOLOR
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11835.06

構造登録者

Zdanowski, K.,Pecqueur, L.,Werner, J.,Potts, J.R.,Kleanthous, C. (登録日: 2015-12-17, 公開日: 2016-08-03, 最終更新日: 2024-11-13)

主引用文献

Rajasekar, K.V.,Zdanowski, K.,Yan, J.,Hopper, J.T.,Francis, M.L.,Seepersad, C.,Sharp, C.,Pecqueur, L.,Werner, J.M.,Robinson, C.V.,Mohammed, S.,Potts, J.R.,Kleanthous, C.
The Anti-Sigma Factor Rsra Responds to Oxidative Stress by Reburying its Hydrophobic Core.
Nat.Commun., 7:12194-, 2016

PubMed Abstract: Redox-regulated effector systems that counteract oxidative stress are essential for all forms of life. Here we uncover a new paradigm for sensing oxidative stress centred on the hydrophobic core of a sensor protein. RsrA is an archetypal zinc-binding anti-sigma factor that responds to disulfide stress in the cytoplasm of Actinobacteria. We show that RsrA utilizes its hydrophobic core to bind the sigma factor σ(R) preventing its association with RNA polymerase, and that zinc plays a central role in maintaining this high-affinity complex. Oxidation of RsrA is limited by the rate of zinc release, which weakens the RsrA-σ(R) complex by accelerating its dissociation. The subsequent trigger disulfide, formed between specific combinations of RsrA's three zinc-binding cysteines, precipitates structural collapse to a compact state where all σ(R)-binding residues are sequestered back into its hydrophobic core, releasing σ(R) to activate transcription of anti-oxidant genes.

PubMed: 27432510
DOI: 10.1038/NCOMMS12194

実験手法

SOLUTION NMR