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Formylglycine generating enzyme from T. curvata in complex with Cd(II)
Structural highlights
FunctionFGE_THECD Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins. 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile.[1] [2] Publication Abstract from PubMedThe formylglycine-generating enzyme (FGE) is a unique copper protein that catalyzes oxygen-dependent C-H activation. We describe 1.66 A- and 1.28 A-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. Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme.,Meury M, Knop M, Seebeck FP Angew Chem Int Ed Engl. 2017 Jul 3;56(28):8115-8119. doi: 10.1002/anie.201702901., Epub 2017 Jun 9. PMID:28544744[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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