Science (American Association for the Advancement of Science), 1997-10, Vol.278 (5339), p.853-856
1997
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Details
- Autor(en) / Beteiligte
- Titel
- Metal Ion Chaperone Function of the Soluble Cu(I) Receptor Atx1
- Ist Teil von
- Science (American Association for the Advancement of Science), 1997-10, Vol.278 (5339), p.853-856
- Ort / Verlag
- Washington, DC: American Society for the Advancement of Science
- Erscheinungsjahr
- 1997
- Quelle
- American Association for the Advancement of Science
- Beschreibungen/Notizen
- 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(l) 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0036-8075eISSN: 1095-9203DOI: 10.1126/science.278.5339.853Titel-ID: cdi_proquest_miscellaneous_743701714
- Format
- –
- Schlagworte
- Amino Acid Sequence, Amino acids, Bioavailability, Biochemistry, Biological and medical sciences, Carrier Proteins, Cation Transport Proteins, Cells, Chemical bonding, Classical genetics, quantitative genetics, hybrids, Coordination, Copper, Copper (Nutrient), Copper - metabolism, Copper in the body, Cytology, Data lines, Disease, Environment, Escherichia coli, Fundamental and applied biological sciences. Psychology, Fungal Proteins - metabolism, Fungal Proteins - physiology, Genetics of eukaryotes. Biological and molecular evolution, Geometry, Humans, Ions, Ligands, Metal ions, Metals, Molecular Chaperones - physiology, Molecular dynamics, Molecular Sequence Data, Molecular structure, Observations, Organic Chemistry, Proteins, Recombinant Proteins, Saccharomyces cerevisiae - metabolism, Saccharomyces cerevisiae - physiology, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Spectroscopy, Sulfur, Thallophyta, bryophyta, Thiols, Transport proteins, Vegetals, Yeast, Yeasts