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

Proteins. 2012 Jun;80(6):1694-8. doi: 10.1002/prot.24050. Epub 2012 Mar 20.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallography, X-Ray
  • Cysteine / chemistry
  • Cysteine / metabolism
  • Humans
  • Mice
  • Mitochondrial Proteins
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Receptor Coactivators / chemistry
  • Oxidation-Reduction
  • Protein Structure, Tertiary
  • Proteins / chemistry
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Zebrafish / metabolism*
  • Zebrafish Proteins / chemistry*
  • Zebrafish Proteins / metabolism


  • Mitochondrial Proteins
  • NCOA7 protein, human
  • Nuclear Receptor Coactivators
  • OXR1 protein, human
  • Proteins
  • Zebrafish Proteins
  • Cysteine