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

Nature Structural Biology volume 5, pages 400–406 (1998)Cite this article

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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Authors and Affiliations

  1. Division of Protein Engineering, Korea Research Institute of Bioscience and Biotechnology, KIST, P.O.Box 115, Yusong,Taejon, 305-600, South Korea

    Hee-Jeong Choi & Seong-Eon Ryu

  2. Laboratory of Cell Signaling, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, 20892, USA

    Sang Won Kang & Sue Goo Rhee

  3. Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul, 151-742, South Korea

    Hee-Jeong Choi & Chul-Hak Yang

Authors
  1. Hee-Jeong Choi
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  4. Sue Goo Rhee
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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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