Atx1-like chaperones and their cognate P-type ATPases: copper-binding and transfer |
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Authors: | Chloe Singleton Nick E. Le Brun |
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Affiliation: | (1) Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich, NR4 7TJ, UK |
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Abstract: | Copper is an essential yet toxic metal ion. To satisfy cellular requirements, while, at the same time, minimizing toxicity, complex systems of copper trafficking have evolved in all cell types. The best conserved and most widely distributed of these involve Atx1-like chaperones and P1B-type ATPase transporters. Here, we discuss current understanding of how these chaperones bind Cu(I) and transfer it to the Atx1-like N-terminal domains of their cognate transporter. |
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Keywords: | Copper trafficking Chaperone P-type ATPase Copper transfer Atx1 CopZ |
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