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Related Experiment Videos

Yeast cox17 solution structure and Copper(I) binding.

Carnie Abajian1, Liliya A Yatsunyk, Benjamin E Ramirez

  • 1Department of Biochemistry, Northwestern University, Evanston, IL 60208, USA.

The Journal of Biological Chemistry
|October 7, 2004
PubMed
Summary
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Cox17, a copper chaperone, delivers copper to cytochrome c oxidase. Structural studies reveal its unique design for interacting with Sco1 and Cox11 proteins.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Cox17 is a copper-binding protein involved in copper delivery to cytochrome c oxidase.
  • It facilitates copper transfer via Sco1 and Cox11 proteins.

Purpose of the Study:

  • To elucidate the structural and binding characteristics of Cox17.
  • To understand its role as a copper chaperone.

Main Methods:

  • Isothermal titration calorimetry (ITC) to determine copper binding affinity.
  • Nuclear Magnetic Resonance (NMR) spectroscopy to determine solution structures of apo and copper-loaded Cox17.

Main Results:

  • Cox17 binds one Cu(I) ion with high affinity (K(a) = 6.15 x 10^6 M^-1).

Related Experiment Videos

  • Solution structures reveal an unstructured N-terminal region and two alpha helices.
  • Copper binding induces ordering in the copper-binding region, with Cu(I) ligated by Cys23 and Cys26.
  • Positively charged residues suggest specific interactions with Sco1 and Cox11.

    • Conclusions:

    • Cox17 is structurally optimized for its copper chaperone function.
    • Its design facilitates specific interactions with two distinct target proteins, Sco1 and Cox11.
    • This highlights Cox17's specialized role in cellular copper trafficking.