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Publication Abstract from PubMed

Bacteria possess cytosolic proteins (Csp3s) capable of binding large quantities of copper and preventing toxicity. Crystal structures of a Csp3 plus increasing amounts of CuI provide atomic-level information about how a storage protein loads with metal ions. Many more sites are occupied than CuI equiv added, with binding by twelve central sites dominating. These can form [Cu4 (S-Cys)4 ] intermediates leading to [Cu4 (S-Cys)5 ]- , [Cu4 (S-Cys)6 ]2- , and [Cu4 (S-Cys)5 (O-Asn)]- clusters. Construction of the five CuI sites at the opening of the bundle lags behind the main core, and the two least accessible sites at the opposite end of the bundle are occupied last. Facile CuI cluster formation, reminiscent of that for inorganic complexes with organothiolate ligands, is largely avoided in biology but is used by proteins that store copper in the cytosol of prokaryotes and eukaryotes, where this reactivity is also key to toxicity.

Visualizing Biological Copper Storage: The Importance of Thiolate-Coordinated Tetranuclear Clusters.,Basle A, Platsaki S, Dennison C Angew Chem Int Ed Engl. 2017 Jul 17;56(30):8697-8700. doi:, 10.1002/anie.201703107. Epub 2017 Jun 19. PMID:28504850^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.