Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution

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Title
Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution
Author(s)
Hee Jeong Choi; Sang Won Kang; Chul Hak Yang; Sue Goo Rhee; Seong Eon Ryu
Bibliographic Citation
Nature Structural & Molecular Biology, vol. 5, no. 5, pp. 400-406
Publication Year
1998
Abstract
Hydrogen peroxide (H2O2) has been implicated recently as an intracellular messenger that affects cellular processes including protein phosphorylation, transcription and apoptosis. A set of novel peroxidases, named peroxiredoxins (Prx), regulate the intracellular concentration of H2O2 by reducing it in the presence of an appropriate electron donor. The crystal structure of a human Prx enzyme, hORF6, reveals that the protein contains two discrete domains and forms a dimer. The N-terminal domain has a thioredoxin fold and the C-terminal domain is used for dimerization. The active site cysteine (Cys 47), which exists as cysteine-sulfenic acid in the crystal, is located at the bottom of a relatively narrow pocket. The positively charged environment surrounding Cys 47 accounts for the peroxidase activity of the enzyme, which contains no redox cofactors.
ISSN
1072-8368
Publisher
Springer-Nature Pub Group
DOI
http://dx.doi.org/10.1038/nsb0598-400
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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