Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate O₂ activation.

ABSTRACT: The formylglycine-generating enzyme (FGE) is required for the posttranslational activation of type I sulfatases by oxidation of an active-site cysteine to C_α-formylglycine. FGE has emerged as an enabling biotechnology tool due to the robust utility of the aldehyde product as a bioconjugation handle in recombinant proteins. Here, we show that Cu(I)-FGE is functional in O₂ activation and reveal a high-resolution X-ray crystal structure of FGE in complex with its catalytic copper cofactor. We establish that the copper atom is coordinated by two active-site cysteine residues in a nearly linear geometry, supporting and extending prior biochemical and structural data. The active cuprous FGE complex was interrogated directly by X-ray absorption spectroscopy. These data unamb

SUBMITTER: Appel MJ 

PROVIDER: S-EPMC6431200 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature