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- Title
Metal ion chaperone function of the soluble Cu(I) receptor Atx1.
- Authors
Pufahl, R A; Singer, C P; Peariso, K L; Lin, S J; Schmidt, P J; Fahrni, C J; Culotta, V C; Penner-Hahn, J E; O'Halloran, T V
- 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.
- Publication
Science (New York, N.Y.), 1997, Vol 278, Issue 5339, p853
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.278.5339.853