| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1178985 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2009 | 7 Pages |
Artemia cysts can tolerate extreme environments, partly due to a heat-stable protein called artemin. According to previous studies, artemin shares structural similarity with ferritins. Actually, there is still no strong structural information about artemin three-dimensional (3-D) structure. In this research, the artemin encoding gene from Artemia urmiana was cloned and sequenced. A reliable 3-D model of artemin was initially built using ferritin as template and refined using Molecular Dynamic (MD) Simulation. It is interesting that the proposed model, confirmed by circular dichroism (CD), shows significant differences in secondary structure contents with ferritin. Three conserved regions (ferroxidase center, iron nucleation center and 3-fold channel) in ferritins, cooperating in iron-interaction, have been substantially changed in artemin. Analysis of C-terminal region of the model revealed its major role in preventing artemin from iron-binding due to some suitable interactions. Finally, it is concluded that significant differences between artemin and ferritin, both in conserved regions related to iron-interaction and three-dimensional structure, can justify their functional differences.
