Structural basis of the redox switch in the OxyR transcription factor

被引:431
作者
Choi, HJ
Kim, SJ
Mukhopadhyay, P
Cho, S
Woo, JR
Storz, G
Ryu, SE
机构
[1] Korea Res Inst Biosci & Biotechnol, Ctr Cellular Switch Prot Struct, Taejon 305600, South Korea
[2] NICHHD, Cell Biol & Metab Branch, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1016/S0092-8674(01)00300-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom and 2.3 Angstrom resolutions, respectively. In the reduced form, the two redox-active cysteines are separated by approximately 17 Angstrom. 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.
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收藏
页码:103 / 113
页数:11
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