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Analysis of the Structure and Function of YfcG from Escherichia coli Reveals an Efficient and Unique Disulfide Bond Reductase

Published

Author(s)

Megan C. Wadington , Jane E. Ladner, N V. Stourman, Joel M. Harp, R N. Armstrong

Abstract

YfcG is one of eight glutathione (GSH) transferase homologues encoded in the Escherichia coli genome. The protein exhibits low or no GSH transferase activity toward a panel of electrophilic substrates. In contrast, it has a very robust disulfidebond reductase activity toward 2-hydroxyethyldisulfide on par with mammalian and bacterial glutaredoxins. The structure of YfcG at 2.3 Å-resolution from crystals grown in the presence of GSH reveals a molecule of glutathione disulfide in the active site. The crystallographic results and the lack of functional cysteine residues in the active site of YfcG suggests that the reductase activity is unique in that no sulfhydryl groups on YfcG are covalently involved in the redox chemistry.
Citation
Biochemistry
Volume
48
Issue
28

Keywords

protein structure, glutathione transferase, disulfidebond reductase, YfcG

Citation

Wadington, M. , Ladner, J. , Stourman, N. , Harp, J. and Armstrong, R. (2009), Analysis of the Structure and Function of YfcG from Escherichia coli Reveals an Efficient and Unique Disulfide Bond Reductase, Biochemistry (Accessed April 13, 2024)
Created July 20, 2009, Updated October 12, 2021