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Updated: Jul 11, 2026
14:44
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
A multinuclear copper(I) cluster forms the dimerization interface in copper-loaded human copper chaperone for
Jay P Stasser1, Gnana S Siluvai, Amanda N Barry
1Department of Environmental and Biomolecular Systems, OGI School of Science and Engineering, Oregon Health and Sciences University, Beaverton, OR 97006-8291, USA.
Biochemistry
|October 2, 2007
Summary
Copper chaperone for superoxide dismutase (CCS) uses a copper cluster to bind and deliver copper to SOD1. This study reveals the cluster
Area of Science:
- Biochemistry
- Metalloprotein Chemistry
- Structural Biology
Background:
- Human copper chaperone for superoxide dismutase (hCCS) is essential for copper delivery to SOD1.
- Previous studies indicated copper coordination within the CXC motif of hCCS.
Purpose of the Study:
- To investigate the role of specific cysteine residues in copper binding and cluster formation in hCCS.
- To elucidate the structural and functional implications of copper cluster formation on hCCS oligomerization and activity.
Main Methods:
- X-ray absorption spectroscopy (XAS) was used to study copper binding.
- Site-directed mutagenesis was employed to create Cys to Ala mutants in hCCS.
- Analysis of copper cluster nuclearity and its effect on protein oligomerization.
Main Results:
- Single Cys to Ala mutations in the D3 CSC motif abolished copper cluster formation and significantly reduced hCCS activity.
- XAS data suggested a Cu4S6 adamantane-type copper cluster.
- Copper binding induced a conformational change, converting the apo dimer to a cluster-linked dimer, maintaining an interface for SOD1 binding.
Conclusions:
- The copper cluster is integral to the reactive form of hCCS.
- Copper loading and cluster formation dictate hCCS oligomerization states.
- The structural integrity of the copper cluster is crucial for hCCS function in copper delivery to SOD1.
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