超氧化物歧化酶与其金属伴侣蛋白复合物的异二聚体结构。
Heterodimeric structure of superoxide dismutase in complex with its metallochaperone.
作者信息
Lamb A L, Torres A S, O'Halloran T V, Rosenzweig A C
机构信息
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.
出版信息
Nat Struct Biol. 2001 Sep;8(9):751-5. doi: 10.1038/nsb0901-751.
The copper chaperone for superoxide dismutase (CCS) activates the eukaryotic antioxidant enzyme copper, zinc superoxide dismutase (SOD1). The 2.9 A resolution structure of yeast SOD1 complexed with yeast CCS (yCCS) reveals that SOD1 interacts with its metallochaperone to form a complex comprising one monomer of each protein. The heterodimer interface is remarkably similar to the SOD1 and yCCS homodimer interfaces. Striking conformational rearrangements are observed in both the chaperone and target enzyme upon complex formation, and the functionally essential C-terminal domain of yCCS is well positioned to play a key role in the metal ion transfer mechanism. This domain is linked to SOD1 by an intermolecular disulfide bond that may facilitate or regulate copper delivery.
超氧化物歧化酶的铜伴侣蛋白（CCS）可激活真核生物抗氧化酶铜锌超氧化物歧化酶（SOD1）。与酵母CCS（yCCS）复合的酵母SOD1的2.9埃分辨率结构表明，SOD1与其金属伴侣蛋白相互作用形成一个由每种蛋白质的一个单体组成的复合物。异二聚体界面与SOD1和yCCS同二聚体界面非常相似。在复合物形成时，伴侣蛋白和靶酶中均观察到显著的构象重排，并且yCCS功能上必不可少的C末端结构域在金属离子转移机制中处于有利位置以发挥关键作用。该结构域通过分子间二硫键与SOD1相连，这可能有助于或调节铜的传递。
Zotero 插件