Download MendeleyA tetranuclear Cu(I) cluster in the metallochaperone protein CopZ.
Hearnshaw, S., West, C., Singleton, C., Zhou, L., Kihlken, M.A., Strange, R.W., Le Brun, N.E., Hemmings, A.M.(2009) Biochemistry 48: 9324-9326
- PubMed: 19746989
- DOI: https://doi.org/10.1021/bi9011995
- Primary Citation of Related Structures:
2QIF - PubMed Abstract:
Copper trafficking proteins and copper-sensitive regulators are often found to be able to bind multiple Cu(I) ions in the form of Cu(I) clusters. We have determined the high-resolution X-ray crystal structure of an Atx1-like copper chaperone protein from Bacillus subtilis containing a novel tetranuclear Cu(I) cluster. The identities and oxidation states of the cluster ions were established unambiguously by refinement of X-ray energy-dependent anomalous scattering factors. The [Cu(4)(S-Cys)(4)(N-His)(2)] cluster geometry provides new structural insights into not only the binding of multiple cuprous ions by metallochaperones but also protein-associated tetranuclear Cu(I) clusters, including those found in eukaryotic copper-responsive transcription factors.
Organizational Affiliation:
Centre for Molecular and Structural Biochemistry, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.
