The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction

Nat Chem Biol. 2006 Jul;2(7):367-8. doi: 10.1038/nchembio797. Epub 2006 May 28.

Abstract

Cellular systems allow transition-metal ions to reach or leave the cell or intracellular locations through metal transfer between proteins. By coupling mutagenesis and advanced NMR experiments, we structurally characterized the adduct between the copper chaperone Atx1 and the first copper(I)-binding domain of the Ccc2 ATPase. Copper was required for the interaction. This study provides an understanding of metal-mediated protein-protein interactions in which the metal ion is essential for the weak, reversible interaction between the partners.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cation Transport Proteins / chemistry*
  • Cation Transport Proteins / genetics
  • Cation Transport Proteins / metabolism*
  • Copper / chemistry*
  • Copper / metabolism*
  • Copper Transport Proteins
  • Ligands
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Binding
  • Protein Structure, Quaternary
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • ATX1 protein, S cerevisiae
  • CCC2 protein, S cerevisiae
  • Carrier Proteins
  • Cation Transport Proteins
  • Copper Transport Proteins
  • Ligands
  • Saccharomyces cerevisiae Proteins
  • Copper