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Researchers revealed the structure of the copper transporter Ctr1 (C-1), essential for cellular copper uptake. This discovery clarifies how cells selectively import copper ions, offering insights into diseases linked to copper imbalance.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Physiology

Background:

  • Copper (Cu) is vital for development, but abnormal levels link to diseases like anemia, metabolic disorders, and cancer.
  • The Ctr1 transporter facilitates cellular copper uptake and distribution, yet its ion selectivity mechanism remains unclear.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying copper ion (Cu+) selectivity in the Ctr1 transporter.
  • To provide high-resolution structural insights into Cu+ import across cell membranes.

Main Methods:

  • X-ray crystallography was used to determine the structures of Salmo salar Ctr1 in both Cu+-free and Cu+-bound states.
  • Functional characterization of Ctr1 was performed alongside structural analysis.

Main Results:

  • The study revealed Ctr1 as a homo-trimeric channel with Cu+-selective properties.
  • Two methionine triad layers were identified as the selectivity filter, coordinating two Cu+ ions near the extracellular entrance.

Conclusions:

  • The high-resolution structures provide a detailed understanding of Cu+ permeation through Ctr1.
  • These findings suggest potential therapeutic strategies for diseases involving aberrant copper accumulation.