A Tetranuclear Cu(I) Cluster in the Metallochaperone Protein CopZ

Hearnshaw, S, West, C, Singleton, C, Zhou, L, Kihlken, MA, Strange, RW, Le Brun, NE and Hemmings, AM (2009) A Tetranuclear Cu(I) Cluster in the Metallochaperone Protein CopZ. Biochemistry, 48 (40). pp. 9324-9326. ISSN 0006-2960

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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 [Cu4(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.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
Faculty of Science > School of Chemistry
Related URLs:
Depositing User: Deborah Clemitshaw
Date Deposited: 12 Sep 2011 10:51
Last Modified: 12 Dec 2018 10:30
URI: https://ueaeprints.uea.ac.uk/id/eprint/25387
DOI: 10.1021/bi9011995

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