Copper chaperones: function, structure and copper-binding properties
Copper chaperones: function, structure and copper-binding properties
复制标题
DOI：
10.1007/s007750050297
复制
发表时间：
1999-04-01
影响因子：
3
通讯作者：
Dameron, CT
中科院分区：
文献类型：
--
作者：
Harrison, MD;Jones, CE;Dameron, CT
铜是生命系统的绝对需要，这种金属在细胞内运输到依赖铜的蛋白质是正常细胞代谢的基础。铜伴侣具有转运和防止铜离子在转运过程中的细胞质暴露的双重功能。目前只发现了少量的铜伴侣蛋白，但它们在植物、细菌和动物物种中的保存表明，大多数生命系统都利用这些蛋白质进行铜路由。现有的数据表明，细胞中的每一种铜依赖蛋白都由一种特定的铜伴侣蛋白提供服务。尽管铜伴侣蛋白在特定细胞类型中不能相互替代，但在不同细胞类型中传递相同蛋白质的铜伴侣蛋白在功能上似乎是相同的。迄今为止发现的大多数铜伴侣蛋白都具有“开放面β -三明治”的全局褶皱，具有保守的MXCXXC金属结合基序。铜依赖性蛋白的特异性似乎是由铜结合基序周围的残基介导的。铜与铜(I)等蛋白质结合，形成三种含硫配体的三角络合物。只有细胞色素c-氧化酶特异性的铜伴侣Cox17偏离了这种设计。
Copper is an absolute requirement for living systems and the intracellular trafficking of this metal to copper-dependent proteins is fundamental to normal cellular metabolism. The copper chaperones perform the dual functions of trafficking and the prevention of cytoplasmic exposure to copper ions in transit. Only a small number of copper chaperones have been identified at this time but their conservation across plant, bacterial and animal species suggests that the majority of living systems utilise these proteins for copper routing. The available data suggest that each copper-dependent protein in the cell is served by a specific copper chaperone. Although copper chaperones cannot be substituted for one another in a given cell type, copper chaperones that deliver to the same protein in different cell types appear to be functionally equivalent. The majority of the copper chaperones identified thus far have an "open-faced beta-sandwich" global fold with a conserved MXCXXC metal-binding motif. Specificity for a given copper-dependent protein appears to be mediated by the residues surrounding the copper-binding motif. Copper binds to such proteins as Cu(I) in a trigonal complex with three sulfur ligands. Only the copper chaperone specific for cytochrome-c-oxidase, Cox17, deviates from this design.