Purification, crystallization and preliminary crystallographic studies of the TLDc domain of oxidation resistance protein 2 from zebrafish
- Authors
- Alsarraf, H.M., Laroche, F., Spaink, H., Thirup, S., and Blaise, M.
- ID
- ZDB-PUB-111129-8
- Date
- 2011
- Source
- Acta crystallographica. Section F, Structural biology and crystallization communications 67(10): 1253-1256 (Journal)
- Registered Authors
- Spaink, Herman P.
- Keywords
- oxidation resistance proteins, TLDc domain
- MeSH Terms
-
- Animals
- Carrier Proteins/chemistry*
- Carrier Proteins/isolation & purification
- Crystallization
- Crystallography, X-Ray
- Models, Molecular
- Protein Structure, Tertiary
- Zebrafish*
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/isolation & purification
- PubMed
- 22102041 Full text @ Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Cell metabolic processes are constantly producing reactive oxygen species (ROS), which have deleterious effects by triggering, for example, DNA damage. Numerous enzymes such as catalase, and small compounds such as vitamin C, provide protection against ROS. The TLDc domain of the human oxidation resistance protein has been shown to be able to protect DNA from oxidative stress; however, its mechanism of action is still not understood and no structural information is available on this domain. Structural information on the TLDc domain may therefore help in understanding exactly how it works. Here, the purification, crystallization and preliminary crystallographic studies of the TLDc domain from zebrafish are reported. Crystals belonging to the orthorhombic space group P21212 were obtained and diffracted to 0.97 Å resolution. Selenomethionine-substituted protein could also be crystallized; these crystals diffracted to 1.1 Å resolution and the structure could be solved by SAD/MAD methods.