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Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish

Authors

  • Mickaël Blaise,

    Corresponding author
    1. Department of Molecular Biology and Genetics, Centre for Carbohydrate Recognition and Signalling, Aarhus University, Aarhus, Denmark
    • Department of Molecular Biology and Genetics, Centre for Carbohydrate Recognition and Signalling, Gustav Wieds vej 10c, Aarhus University, Aarhus Denmark
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  • Husam M. A. B. Alsarraf,

    1. Department of Molecular Biology and Genetics, Centre for Carbohydrate Recognition and Signalling, Aarhus University, Aarhus, Denmark
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  • Jaslyn E. M. M. Wong,

    1. Department of Molecular Biology and Genetics, Centre for Carbohydrate Recognition and Signalling, Aarhus University, Aarhus, Denmark
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  • Søren Roi Midtgaard,

    1. Nanobioscience Group, Faculty of LIFE Sciences, University of Copenhagen, Copenhagen, Denmark
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  • Fabrice Laroche,

    1. Department of Molecular Biology and Genetics, Centre for Carbohydrate Recognition and Signalling, Aarhus University, Aarhus, Denmark
    2. Institute of Biology, Leiden University, Leiden, The Netherlands
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  • Lotte Schack,

    1. Department of Molecular Biology and Genetics, Centre for Carbohydrate Recognition and Signalling, Aarhus University, Aarhus, Denmark
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  • Herman Spaink,

    1. Department of Molecular Biology and Genetics, Centre for Carbohydrate Recognition and Signalling, Aarhus University, Aarhus, Denmark
    2. Institute of Biology, Leiden University, Leiden, The Netherlands
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  • Jens Stougaard,

    1. Department of Molecular Biology and Genetics, Centre for Carbohydrate Recognition and Signalling, Aarhus University, Aarhus, Denmark
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  • Søren Thirup

    1. Department of Molecular Biology and Genetics, Centre for Carbohydrate Recognition and Signalling, Aarhus University, Aarhus, Denmark
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Abstract

The oxidation resistance proteins (OXR) help to protect eukaryotes from reactive oxygen species. The sole C-terminal domain of the OXR, named TLDc is sufficient to perform this function. However, the mechanism by which oxidation resistance occurs is poorly understood. We present here the crystal structure of the TLDc domain of the oxidation resistance protein 2 from zebrafish. The structure was determined by X-ray crystallography to atomic resolution (0.97Å) and adopts an overall globular shape. Two antiparallel β-sheets form a central β-sandwich, surrounded by two helices and two one-turn helices. The fold shares low structural similarity to known structures. Proteins 2012. © 2012 Wiley Periodicals, Inc.

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