Construction of a novel metal accumulating protein using the plant ferritin as a scaffold

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We have attempted to elucidate the structure and function of plant ferritins. The most prominent feature of the plant ferritin is the extension peptide(EP) in the N-terminus of plant ferritin. The structural analysis of UpFER at 2. 4 A resolution revealed the precise structure and its interaction with the conserved region which forms the oligomeric protein shell. It was also suggested that the removal of the EP from plant ferritin made the protein shell more unstable and hydrophobic, which induce the aggregation and degradation of the ferritin shell. Another experiment was performed on a novel calcium binding protein. To elucidate the mechanism in calcium storage, we have attempted to solve the three dimensional structure of this protein. As result, we determined the structure of this protein at 1. 6 A resolution. Some calcium ions were visible in the electron density map, and we are evaluating the structure and function of this protein.