| Literature DB >> 22434723 |
Mickaël Blaise1, Husam M A B Alsarraf, Jaslyn E M M Wong, Søren Roi Midtgaard, Fabrice Laroche, Lotte Schack, Herman Spaink, Jens Stougaard, Søren Thirup.
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.Entities:
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Year: 2012 PMID： 22434723 DOI： 10.1002/prot.24050
Source DB: PubMed Journal: Proteins ISSN： 0887-3585