Copper (Cu+) transporters of the Ctr family are sequence diverse eukaryotic proteins that function by an unknown mechanism of action. We have conducted bioinformatic analyses of sequenced Ctr proteins. Multiple paralogues are found in single organisms, and these may be either closely or distantly related to each other. Protein phylogeny generally correlates with organismal source and protein size with proteins of each cluster being derived from a specific eukaryotic kingdom and exhibiting characteristic domain arrangements. Some homologues exhibit repeats of the basic 3 TMS unit. Regions of conserved hydrophobicity and amphipathicity suggest functional roles, particularly for putative TMSs 2 and 3 which possess a nearly fully conserved M X3 M motif in putative TMS2. We propose that this motif comprises the transmembrane Cu+-binding site in oligomeric channels that take up Cu+ by a passive, membrane potential-dependent mechanism.

Journal Section:
Review
Keywords:
Heavy metals, Transport, Channels, Copper, Cuprous ions, Binding motif
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© 2006 S. Karger AG, Basel
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2006
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