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

doi:10.1126/science.278.5339.853

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^*

^*Corresponding author for this work

Chemistry

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623 Scopus citations

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 language	English (US)
Pages (from-to)	853-856
Number of pages	4
Journal	Science
Volume	278
Issue number	5339
DOIs	https://doi.org/10.1126/science.278.5339.853
State	Published - Oct 31 1997

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title = "Metal ion chaperone function of the soluble Cu(I) receptor Atx1",

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.",

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

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T1 - Metal ion chaperone function of the soluble Cu(I) receptor Atx1

AU - Pufahl, R. A.

AU - Singer, C. P.

AU - Peariso, K. L.

AU - Lin, S. J.

AU - Schmidt, P. J.

AU - Fahrni, C. J.

AU - Cizewski Culotta, V.

AU - Penner-Hahn, J. E.

AU - O'Halloran, T. V.

PY - 1997/10/31

Y1 - 1997/10/31

N2 - 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.

AB - 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.

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

Abstract

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