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

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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 [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.

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Original languageEnglish
Pages (from-to)9324-9326
Number of pages3
JournalBiochemistry
Volume48
Issue number40
DOIs
Publication statusPublished - 11 Sep 2009
Peer-reviewedYes

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