2b7j
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Crystal Structure of Yeast Sco1 with Copper Bound
OverviewOverview
The Sco family of proteins are involved in the assembly of the dinuclear, CuA site in cytochrome c oxidase (COX), the terminal enzyme in aerobic, respiration. These proteins, which are found in both eukaryotes and, prokaryotes, are characterized by a conserved CXXXC sequence motif that, binds copper ions and that has also been proposed to perform a, thiol:disulfide oxidoreductase function. The crystal structures of, Saccharomyces cerevisiae apo Sco1 (apo-ySco1) and Sco1 in the presence of, copper ions (Cu-ySco1) were determined to 1.8- and 2.3-A resolutions, respectively. Yeast Sco1 exhibits a thioredoxin-like fold, similar to that, observed for human Sco1 and a homolog from Bacillus subtilis. The Cu-ySco1, structure, obtained by soaking apo-ySco1 crystals in copper ions, reveals, an unexpected copper-binding site involving Cys181 and Cys216, cysteine, residues present in ySco1 but not in other homologs. The conserved CXXXC, cysteines, Cys148 and Cys152, can undergo redox chemistry in the crystal., An essential histidine residue, His239, is located on a highly flexible, loop, denoted the Sco loop, and can adopt positions proximal to both pairs, of cysteines. Interactions between ySco1 and its partner proteins yeast, Cox17 and yeast COX2 are likely to occur via complementary electrostatic, surfaces. This high-resolution model of a eukaryotic Sco protein provides, new insight into Sco copper binding and function.
About this StructureAbout this Structure
2B7J is a Single protein structure of sequence from Saccharomyces cerevisiae with CU as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of yeast Sco1., Abajian C, Rosenzweig AC, J Biol Inorg Chem. 2006 Jun;11(4):459-66. Epub 2006 Mar 29. PMID:16570183
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