Structural highlights
Function[COPZ_BACSU] Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-transporting ATPase CopA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCopper 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. 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, Hemmings AM Biochemistry. 2009 Oct 13;48(40):9324-6. PMID:19746989[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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