A study was conducted to demonstrate crystallographic, solution, and cryoelectron microscopic structures of copper chaperones and membrane-bound copper transporters for all living systems. It was demonstrated that copper transported into eukaryotic cells as Cu(I) by members of the Ctr copper transporter family. These membrane transporters were identified in yeast, plants, humans, and other animals and contained several methionine-rich motifs at their N-termini and conserved cysteine and histidine residues at their C-termini. The Cu(I) transporting PIB-type ATPases consisted of eight transmembrane (TM) helices and cytoplasmic ATP binding (ATPBD). It was also found that the Cu(I) transporting PIB-type ATPases were found in large numbers in prokaryotes.
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