Copper chaperones, intracellular copper trafficking proteins. Function, structure, and mechanism of action

This review summarizes findings on a new family of small cytoplasmic proteins called copper chaperones. The copper chaperones bind and deliver copper ions to intracellular compartments and insert the copper into the active sites of specific partners, copper-dependent enzymes. Three types of copper c...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2003-08, Vol.68 (8), p.827-837
Main Authors: Markossian, K A, Kurganov, B I
Format: Article
Language:English
Subjects:
Animals
Carrier Proteins - metabolism
Cation Transport Proteins - metabolism
Copper
Copper - metabolism
Electron Transport Complex IV - metabolism
Humans
Membrane Proteins - metabolism
Mitochondrial Proteins
Models, Molecular
Molecular Chaperones - metabolism
Protein Transport - physiology
Proteins
Saccharomyces cerevisiae Proteins - metabolism
Superoxide Dismutase - metabolism
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Summary:This review summarizes findings on a new family of small cytoplasmic proteins called copper chaperones. The copper chaperones bind and deliver copper ions to intracellular compartments and insert the copper into the active sites of specific partners, copper-dependent enzymes. Three types of copper chaperones have been found in eukaryotes. Their three-dimensional structures have been determined, intracellular target proteins identified, and mechanisms of action have been revealed. The Atx1 copper chaperone binds Cu(I) and interacts directly with the copper-binding domains of a P-type ATPase copper transporter, its physiological partner. The copper chaperone CCS delivers Cu(I) to Cu,Zn-superoxide dismutase 1. Cox17 and Cox11 proteins serve as copper chaperones for cytochrome c oxidase, a copper-dependent enzyme.
ISSN:0006-2979
1608-3040
DOI:10.1023/A:1025740228888