Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 56, Issue 30, Pages 8697-8700Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201703107
Keywords
bioinorganic chemistry; copper; copper storage; metalloproteins; structural biology
Categories
Funding
- Biotechnology and Biological Sciences Research Council [BB/K008439/1]
- Newcastle University
- Biotechnology and Biological Sciences Research Council [BB/K008439/1] Funding Source: researchfish
- BBSRC [BB/K008439/1] Funding Source: UKRI
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Bacteria possess cytosolic proteins (Csp3s) capable of binding large quantities of copper and preventing toxicity. Crystal structures of a Csp3 plus increasing amounts of Cu-I provide atomic-level information about how a storage protein loads with metal ions. Many more sites are occupied than Cu-I equiv added, with binding by twelve central sites dominating. These can form [Cu-4(S-Cys)(4)] intermediates leading to [Cu-4(S-Cys)(5)](-), [Cu-4(S-Cys)(6)](2-), and [Cu-4(S-Cys)(5)(O-Asn)](-) clusters. Construction of the five Cu-I 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 Cu-I 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.
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