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A structural-dynamical characterization of human Cox17.

Lucia Banci1, Ivano Bertini, Simone Ciofi-Baffoni

  • 1Magnetic Resonance Center Centro Risonanze Magnetiche (CERM) and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.

The Journal of Biological Chemistry
|December 21, 2007
PubMed
Summary
This summary is machine-generated.

Human Cox17, a mitochondrial copper chaperone, delivers copper to cytochrome c oxidase. Its structure and dynamics reveal how copper binding and redox changes facilitate this essential cellular process.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Human Cox17 is a crucial mitochondrial copper chaperone.
  • It facilitates copper delivery to cytochrome c oxidase, vital for cellular respiration.
  • Understanding Cox17's structure and function is key to mitochondrial health.

Purpose of the Study:

  • To structurally and dynamically characterize human Cox17 in its functional states.
  • To elucidate the role of redox and metallation in Cox17's copper-chaperoning activity.
  • To investigate the mechanism of copper delivery to cytochrome c oxidase.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy for structural and dynamical analysis.
  • Characterization of various metallated and redox states of human Cox17.
  • Investigation of disulfide bond formation and copper(I) binding.

Main Results:

  • The NMR solution structure of partially oxidized Cox17 (Cox17(2S-S)) reveals a structured domain and a flexible N-terminal tail.
  • A novel Cys-Cys binding motif for copper(I) was identified in human Cu(I)Cox17(2S-S).
  • Copper(I) binding and disulfide formation induce localized structural and dynamical changes.

Conclusions:

  • The fully reduced Cox17 is unstructured in the cytoplasm and becomes partially structured upon oxidation to Cox17(2S-S) in the intermembrane space (IMS).
  • Cox17(2S-S) is the functional IMS species, capable of binding one copper(I) ion for delivery to cytochrome c oxidase.
  • The copper(I) form of Cox17(2S-S) exhibits characteristics typical of copper chaperones.