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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The crystal structure of yeast copper thionein: the solution of a long-lasting enigma.
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The crystal structure of yeast copper thionein: the solution of a long-lasting enigma.

机译：酵母铜硫蛋白的晶体结构：持久谜团的溶液。

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摘要

We report here the crystal structure of yeast copper thionein (Cu-MT), determined at 1.44-A resolution. The Cu-MT structure shows the largest known oligonuclear Cu(I) thiolate cluster in biology, consisting of six trigonally and two digonally coordinated Cu(I) ions. This is at variance with the results from previous spectroscopic determinations, which were performed on MT samples containing seven rather than eight metal ions. The protein backbone has a random coil structure with the loops enfolding the copper cluster, which is located in a cleft where it is bound to 10 cysteine residues. The protein structure is somewhat different from that of Ag(7)-MT and similar, but not identical, to that of Cu(7)-MT. Besides the different structure of the metal cluster, the main differences lie in the cysteine topology and in the conformation of some portions of the backbone. The present structure suggests that Cu-MT, in addition to its role as a safe depository for copper ions in the cell, may play an active role in the delivery of copper to metal-free chaperones.
机译：我们在这里报告了以1.44-A分辨率测定的酵母铜硫蛋白（Cu-MT）的晶体结构。 Cu-MT结构显示了生物学上已知的最大的寡核硫酸铜（I）簇，它由六个三角配位和两个三角配位的Cu（I）离子组成。这与以前的光谱测定结果不同，后者是对含有七个而不是八个金属离子的MT样品进行的。蛋白质骨架具有随机的线圈结构，其环圈环绕铜簇，铜簇位于裂口处，与10个半胱氨酸残基结合。蛋白质结构与Ag（7）-MT略有不同，与Cu（7）-MT相似但不相同。除了金属簇的不同结构外，主要区别在于半胱氨酸拓扑结构和主链某些部分的构象。本结构表明，Cu-MT除了作为细胞中铜离子的安全沉积物外，还可能在将铜传递给不含金属的伴侣中发挥积极作用。

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