1i69
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1i69 |SIZE=350|CAPTION= <scene name='initialview01'>1i69</scene>, resolution 2.7Å | |PDB= 1i69 |SIZE=350|CAPTION= <scene name='initialview01'>1i69</scene>, resolution 2.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BEZ:BENZOIC ACID'>BEZ</scene> | + | |LIGAND= <scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1i6a|1I6A]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i69 OCA], [http://www.ebi.ac.uk/pdbsum/1i69 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i69 RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Kim, S.]] | [[Category: Kim, S.]] | ||
[[Category: Ryu, S.]] | [[Category: Ryu, S.]] | ||
| - | [[Category: BEZ]] | ||
[[Category: oxyr regulatory domain]] | [[Category: oxyr regulatory domain]] | ||
[[Category: reduced form]] | [[Category: reduced form]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:15:09 2008'' |
Revision as of 18:15, 30 March 2008
| |||||||
| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1I6A
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Escherichia coli. Full crystallographic information is available from 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:11301006
Page seeded by OCA on Sun Mar 30 21:15:09 2008
