Pufahl RA, et al. (1997) Metal ion chaperone function of the soluble Cu(I) receptor Atx1. Science 278(5339):853-6
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.
|Status: Published||Type: Journal Article||PubMed ID: 9346482|
Topics addressed in this paper
Number of different genes curated to this paper: 2
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