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A structural perspective on copper uptake in eukaryotes.

Christopher J De Feo1, Stephen G Aller, Vinzenz M Unger

  • 1Department of Molecular Biophysics and Biochemistry, Yale School of Medicine, P.O. Box 208024, New Haven, CT 06520-8024, USA.

Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine
|January 11, 2007
PubMed
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Genetic studies identified copper transporters (CTRs) essential for cellular copper uptake. Electron crystallography revealed the human high-affinity transporter (hCTR1) has a trimeric structure with a central pore, suggesting a channel-like mechanism for copper transport.

Area of Science:

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Copper transporters (CTRs) are integral membrane proteins crucial for cellular copper uptake.
  • Genetic studies have established CTRs as essential for this process.
  • Previous research identified a family of CTRs, including the high-affinity human transporter hCTR1.

Purpose of the Study:

  • To determine the structure of the human high-affinity copper transporter (hCTR1) using electron crystallography.
  • To elucidate the structural basis for hCTR1's function in cellular copper uptake.
  • To explore the implications of hCTR1 structure for the transport of other transition metals.

Main Methods:

  • Electron crystallography was employed to generate a projection density map of hCTR1.

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  • The map was determined at 6 Å resolution for hCTR1 embedded in a lipid bilayer.
  • Structure-function studies were correlated with the obtained projection density map.

    • Main Results:

    • The electron crystallography data revealed hCTR1 forms a trimer.
    • hCTR1 exhibits radial symmetry, characteristic of ion channels.
    • A central low-density region suggests a copper-permeable pore along the trimer's three-fold axis.

    Conclusions:

    • The trimeric structure of hCTR1, with a central pore, provides a structural basis for its role as a copper transporter.
    • The architecture of hCTR1 is analogous to known ion channels.
    • The structural findings offer insights into the cellular uptake mechanisms of other transition metals.