1u96
From Proteopedia
|
Solution Structure of Yeast Cox17 with Copper Bound
Overview
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, 10(6) M(-1). The solution structures of both apo and Cu(I)-loaded Cox17, reveal two alpha 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 Cys(23) and Cys(26). 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.
About this Structure
1U96 is a Single protein structure of sequence from Saccharomyces cerevisiae with CU1 as ligand. Full crystallographic information is available from OCA.
Reference
Yeast cox17 solution structure and Copper(I) binding., Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC, J Biol Chem. 2004 Dec 17;279(51):53584-92. Epub 2004 Oct 1. PMID:15465825
Page seeded by OCA on Wed Nov 21 03:56:11 2007
