Ontology highlight
ABSTRACT:
SUBMITTER: Jonsson TJ
PROVIDER: S-EPMC2785173 | biostudies-literature | 2009 Nov
REPOSITORIES: biostudies-literature
Jönsson Thomas J TJ Johnson Lynnette C LC Lowther W Todd WT
The Journal of biological chemistry 20091006 48
Oxidative stress can damage the active site cysteine of the antioxidant enzyme peroxiredoxin (Prx) to the sulfinic acid form, Prx-SO(2)(-). This modification leads to inactivation. Sulfiredoxin (Srx) utilizes a unique ATP-Mg(2+)-dependent mechanism to repair the Prx molecule. Using selective protein engineering that involves disulfide bond formation and site-directed mutagenesis, a mimic of the enzyme.substrate complex has been trapped. Here, we present the 2.1 A crystal structure of human Srx i ...[more]