Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 56, Issue 28, Pages 8115-8119Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201702901
Keywords
C-H activation; copper chaperone; copper enzyme; enzyme catalysis; formylglycine
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Funding
- Professur fur Molekulare Bionik
- Swiss National Science Foundation
- Commission for Technology an Innovation
- European Research Council
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The formylglycine-generating enzyme (FGE) is a unique copper protein that catalyzes oxygen-dependent C-H activation. We describe 1.66 c-and 1.28 c-resolution crystal structures of FGE from Thermomonospora curvata in complex with either AgI or CdII providing definitive evidence for a high-affinity metal-binding site in this enzyme. The structures reveal a bis-cysteine linear coordination of the monovalent metal, and tetrahedral coordination of the bivalent metal. Similar coordination changes may occur in the active enzyme as a result of CuI/II redox cycling. Complexation of copper atoms by two cysteine residues is common among copper-trafficking proteins, but is unprecedented for redox-active copper enzymes or synthetic copper catalysts.
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