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

我们试图阐明植物铁蛋白的结构和功能。植物铁蛋白最显著的特征是其n端延伸肽（EP）。2. UpFER结构分析。分辨率揭示了其精确的结构及其与形成寡聚蛋白外壳的保守区域的相互作用。从植物铁蛋白中去除EP后，铁蛋白外壳变得更加不稳定和疏水，从而导致铁蛋白外壳的聚集和降解。另一项实验是对一种新的钙结合蛋白进行的。为了阐明钙储存的机制，我们试图解决该蛋白的三维结构。结果，我们确定了该蛋白在1的结构。6 .决议。在电子密度图中可以看到一些钙离子，我们正在评估这种蛋白质的结构和功能。

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.