Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 477, Issue 1, Pages 98-104Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2008.04.036
Keywords
human peroxiredoxin; X-ray crystal structure; oxidized state; antioxidant enzyme; thioredoxin fold; thioredoxin peroxidase; sulfenic acid; benzoate ligand
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Peroxiredoxin 5 (PRDX5) belongs to the PRDX superfamily of thiol-dependent peroxidases able to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. PRDX5 is classified in the atypical 2-Cys sub-family of PRDXs. In this subfamily, the oxidized form of the enzyme is characterized by the presence of an intramolecular disulfide bridge between the peroxidatic and the resolving cysteine residues. We report here three crystal forms in which this intramolecular disulfide bond is indeed observed. The structures are characterized by the expected local unfolding of the peroxidatic loop, but also by the unfolding of the resolving loop. A new type of interface between PRDX molecules is described. The three crystal forms were not oxidized in the same way and the influence of the oxidizing conditions is discussed. (c) 2008 Elsevier Inc. All rights reserved.
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