REVIEW: Copper Chaperones, Intracellular Copper Trafficking Proteins. Function, Structure, and Mechanism of Action

K. A. Markossian^* and B. I. Kurganov

Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, Moscow 119071, Russia; fax: (095) 954-2732; E-mail: markossian@inbi.ras.ru

^* To whom correspondence should be addressed.

Received November 12, 2002; Revision received March 20, 2003

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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.

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KEY WORDS: copper chaperones, P-type ATPase copper transporter, Cu,Zn-superoxide dismutase, cytochrome c oxidase, copper transport

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