A tetranuclear Cu(I) cluster in the metallochaperone protein CopZ

Stephen Hearnshaw, Claire West, Chloe Singleton, Liang Zhou, Margaret A. Kihlken, Richard W. Strange, Nick E. Le Brun, Andrew M. Hemmings

Research output: Contribution to journalArticlepeer-review

30 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)9324-9326
Number of pages3
Issue number40
Publication statusPublished - 11 Sep 2009

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