1I6A

CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF OXYR

1I6A の概要

• エントリーDOI: 10.2210/pdb1i6a/pdb
• 関連するPDBエントリー: 1I69
• 分子名称: HYDROGEN PEROXIDE-INDUCIBLE GENES ACTIVATOR (2 entities in total)
• 機能のキーワード: oxyr regulatory domain, oxidized form, transcription
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24394.31

構造登録者

Choi, H.,Kim, S.,Ryu, S. (登録日: 2001-03-02, 公開日: 2001-09-02, 最終更新日: 2024-11-13)

主引用文献

Choi, H.,Kim, S.,Mukhopadhyay, P.,Cho, S.,Woo, J.,Storz, G.,Ryu, S.
Structural basis of the redox switch in the OxyR transcription factor.
Cell(Cambridge,Mass.), 105:103-113, 2001

PubMed Abstract: The Escherichia coli OxyR transcription factor senses H2O2 and is activated through the formation of an intramolecular disulfide bond. Here we present the crystal structures of the regulatory domain of OxyR in its reduced and oxidized forms, determined at 2.7 A and 2.3 A resolutions, respectively. In the reduced form, the two redox-active cysteines are separated by approximately 17 A. Disulfide bond formation in the oxidized form results in a significant structural change in the regulatory domain. The structural remodeling, which leads to different oligomeric associations, accounts for the redox-dependent switch in OxyR and provides a novel example of protein regulation by "fold editing" through a reversible disulfide bond formation within a folded domain.

PubMed: 11301006
DOI: 10.1016/S0092-8674(01)00300-2

実験手法

X-RAY DIFFRACTION (2.3 Å)