Solution structure of the Apo and copper(I)-loaded human metallochaperone HAH1
Solution structure of the Apo and copper(I)-loaded human metallochaperone HAH1
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DOI：
10.1021/bi0487591
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发表时间：
2004-10-19
期刊：
影响因子：
2.9
通讯作者：
Rosato, A
中科院分区：
文献类型：
--
作者：
Anastassopoulou, I;Banci, L;Rosato, A
人金属配位体HAH1是在大肠杆菌中合成的，在C末端增加了四个氨基酸，并在溶液中用核磁共振波谱进行了表征，包括有无铜(I)。Apo-HAH1单体的溶液结构对主链原子的均方根偏差为0.50埃，对所有重原子的均方根偏差为0.96埃。对于铜(I)-HAH1，这些值分别为0.45埃和0.95埃。铜(I)结合时只有少量的结构重排。特别是，金属结合区周围原子间相互作用的变化仅限于Lys60向金属位置的移动。蛋白质的结构与X射线结晶学在各种衍生物中获得的结构相似，主干RMSD值低于1埃。在全蛋白中，铜(I)被证实是两配位的。如果将这些数据与直系同源蛋白的数据进行比较，我们发现HAH1的配位数从2改变为3的倾向较低。这样的协调切换是铜转移的关键一步。
The human metallochaperone HAH1 has been produced in Escherichia coli with four additional amino acids at the C-terminus and characterized in solution by NMR spectroscopy, both with and without copper(I). The solution structure of the apo-HAH1 monomer has a root-mean-square-deviation (RMSD) of 0.50 Angstrom for the coordinates of the backbone atoms and 0.96 Angstrom for all heavy atoms. These values compare, respectively, with 0.45 and 0.95 Angstrom for copper(I)-HAH1. There are only minor structural rearrangements upon copper(I) binding. In particular, the variation of interatomic interactions around the metal-binding region is limited to a movement of Lys60 toward the metal site. The protein structures are similar to those obtained by X-ray crystallography in a variety of derivatives, with backbone RMSD values below 1 Angstrom. In the holoprotein, copper(I) is confirmed to be two coordinated. If these data are compared with those of orthologue proteins, we learn that HAH1 has a lower tendency to change coordination number from two to three. Such a switch in coordination is a key step in copper transfer.