Heterodimeric structure of superoxide dismutase in complex with its metallochaperone

被引：241

作者：

Lamb, AL

Torres, AS

O'Halloran, TV

Rosenzweig, AC ^{[1
]}

机构：

[1] Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA

[2] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA

来源：

NATURE STRUCTURAL BIOLOGY | 2001年 / 8卷 / 09期

关键词：

D O I：

10.1038/nsb0901-751

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The copper chaperone for superoxide dismutase (CCS) activates the eukaryotic antioxidant enzyme copper, zinc superoxide dismutase (SOD1). The 2.9 Angstrom resolution structure of yeast SOD1 complexed with yeast CCS (yCCS) reveals that SOD I 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 SOD I by an intermolecular disulfide bond that may facilitate or regulate copper delivery.

引用

页码：751 / 755

页数：5

共 47 条

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