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J. Biol. Chem., Vol. 279, Issue 51, 53584-53592, December 17, 2004

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Yeast Cox17 Solution Structure and Copper(I) Binding^*

Carnie Abajian, Liliya A. Yatsunyk, Benjamin E. Ramirez¶, and Amy C. Rosenzweig||

From the Departments of Biochemistry, Molecular Biology, and Cell Biology and of Chemistry and the ^¶Structural Biology NMR Facility, Northwestern University, Evanston, Illinois 60208

Cox17 is a 69-residue cysteine-rich, copper-binding protein that has been implicated in the delivery of copper to the Cu_A and Cu_B centers of cytochrome c oxidase via the copper-binding proteins Sco1 and Cox11, respectively. According to isothermal titration calorimetry experiments, fully reduced Cox17 binds one Cu(I) ion with a K_a of (6.15 ± 5.83) x 10⁶ M^-1. The solution structures of both apo and Cu(I)-loaded Cox17 reveal two helices preceded by an extensive, unstructured N-terminal region. This region is reminiscent of intrinsically unfolded proteins. The two structures are very similar overall with residues in the copper-binding region becoming more ordered in Cu(I)-loaded Cox17. Based on the NMR data, the Cu(I) ion has been modeled as two-coordinate with ligation by conserved residues Cys²³ and Cys²⁶. This site is similar to those observed for the Atx1 family of copper chaperones and is consistent with reported mutagenesis studies. A number of conserved, positively charged residues may interact with complementary surfaces on Sco1 and Cox11, facilitating docking and copper transfer. Taken together, these data suggest that Cox17 is not only well suited to a copper chaperone function but is specifically designed to interact with two different target proteins.

Received for publication, July 16, 2004 , and in revised form, September 29, 2004.

The atomic coordinates and structure factors (codes 1U96 and 1U97) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by National Institutes of Health Grant GM58518. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence may be addressed. Tel.: 847-467-5301; Fax: 847-467-6489; E-mail: amyr{at}northwestern.edu.

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