View source for 1i69

[[Image:1i69.jpg|left|200px]]

 {{Structure
|PDB= 1i69 |SIZE=350|CAPTION= <scene name='initialview01'>1i69</scene>, resolution 2.7&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=BEZ:BENZOIC ACID'>BEZ</scene>
|ACTIVITY= 
|GENE= 
}}

'''CRYSTAL STRUCTURE OF THE REDUCED FORM OF OXYR'''


==Overview==
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.

==About this Structure==
1I69 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I69 OCA]. 

==Reference==
Structural basis of the redox switch in the OxyR transcription factor., Choi H, Kim S, Mukhopadhyay P, Cho S, Woo J, Storz G, Ryu S, Cell. 2001 Apr 6;105(1):103-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11301006 11301006]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Choi, H.]]
[[Category: Kim, S.]]
[[Category: Ryu, S.]]
[[Category: BEZ]]
[[Category: oxyr regulatory domain]]
[[Category: reduced form]]

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