Metal ion chaperone function of the soluble Cu(I) receptor Atx1

R. A. Pufahl, C. P. Singer, K. L. Peariso, S. J. Lin, P. J. Schmidt, C. J. Fahrni, V. Cizewski Culotta, J. E. Penner-Hahn, T. V. O'Halloran

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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.

Original languageEnglish (US)
Pages (from-to)853-856
Number of pages4
JournalScience
Volume278
Issue number5339
DOIs
StatePublished - Oct 31 1997
Externally publishedYes

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    Pufahl, R. A., Singer, C. P., Peariso, K. L., Lin, S. J., Schmidt, P. J., Fahrni, C. J., Cizewski Culotta, V., Penner-Hahn, J. E., & O'Halloran, T. V. (1997). Metal ion chaperone function of the soluble Cu(I) receptor Atx1. Science, 278(5339), 853-856. https://doi.org/10.1126/science.278.5339.853