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

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.

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Correspondence to Seong-Eon Ryu.

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Choi, HJ., Kang, S., Yang, CH. et al. Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution. Nat Struct Mol Biol 5, 400–406 (1998). https://doi.org/10.1038/nsb0598-400

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