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Title 

Structural Basis of the Redox Switch in the OxyR Transcription Factor

Authors 

Hee Jung ChoiSeung Jun KimPartha MunkhopadhyaySa Yeon ChoJoo Rang WooGisela StorzSeong Eon Ryu

Publisher 

Elsevier (Cell Press)

Issue Date 

2001

Citation 

Cell, vol. 105, no. 1, pp. 103-113

Keywords 

transcription factortranscription factor oxyrtranscription regulationtranscription Factors

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 ? and 2.3 ? resolutions, respectively. In the reduced form, the two redox-active cysteines are separated by approximately 17 ?. 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.

ISSN 

0092-8674

Link 

http://dx.doi.org/10.1016/S0092-8674(01)00300-2

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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