Metal Ion Chaperone Function of the Soluble Cu(I) Receptor Atx1
- 31 October 1997
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 278 (5339), 853-856
- https://doi.org/10.1126/science.278.5339.853
Abstract
Reactive and potentially toxic cofactors such as copper ions are imported into eukaryotic cells and incorporated into target proteins by unknown mechanisms. Atx1, a prototypical copper chaperone protein from yeast, has now been shown to act as a soluble cytoplasmic copper(I) receptor that can adopt either a two- or three-coordinate metal center in the active site. Atx1 also associated directly with the Atx1-like cytosolic domains of Ccc2, a vesicular protein defined in genetic studies as a member of the copper-trafficking pathway. The unusual structure and dynamics of Atx1 suggest a copper exchange function for this protein and related domains in the Menkes and Wilson disease proteins.Keywords
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