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 types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Carrier Proteins*
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Cation Transport Proteins*
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Copper / metabolism*
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Copper Transport Proteins
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Escherichia coli
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Fungal Proteins / metabolism
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Fungal Proteins / physiology*
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Humans
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Molecular Chaperones / physiology*
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Molecular Sequence Data
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Recombinant Proteins
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae / physiology*
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
Substances
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ATX1 protein, S cerevisiae
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CCC2 protein, S cerevisiae
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Carrier Proteins
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Cation Transport Proteins
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Copper Transport Proteins
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Fungal Proteins
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Molecular Chaperones
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Recombinant Proteins
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Saccharomyces cerevisiae Proteins
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Copper