1I6A

CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF OXYR

Summary for 1I6A

• Entry DOI: 10.2210/pdb1i6a/pdb
• Related: 1I69
• Descriptor: HYDROGEN PEROXIDE-INDUCIBLE GENES ACTIVATOR (2 entities in total)
• Functional Keywords: oxyr regulatory domain, oxidized form, transcription
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 24394.31

Authors

Choi, H.,Kim, S.,Ryu, S. (deposition date: 2001-03-02, release date: 2001-09-02, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)