Analysis of the structure and function of YfcG from Escherichia coli reveals an efficient and unique disulfide bond reductase.

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TitleAnalysis of the structure and function of YfcG from Escherichia coli reveals an efficient and unique disulfide bond reductase.
Publication TypeJournal Article
Year of Publication2009
AuthorsWadington, MC, Ladner, JE, Stourman, NV, Harp, JM, Armstrong, RN
JournalBiochemistry
Volume48
Issue28
Pagination6559-61
Date Published2009 Jul 21
ISSN1520-4995
KeywordsBinding Sites, Disulfides, Escherichia coli, Escherichia coli Proteins, Fluorescence, Glutathione Disulfide, Glutathione Transferase, Kinetics, Ligands, Models, Molecular, Mutant Proteins, Oxidoreductases, Protein Multimerization, Protein Structure, Secondary, Static Electricity, Substrate Specificity, Sulfhydryl Compounds, Temperature, Titrimetry
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 disulfide-bond reductase activity toward 2-hydroxyethyldisulfide on par with mammalian and bacterial glutaredoxins. The structure of YfcG at 2.3 A-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 in the YfcG protein are covalently involved in the redox chemistry.

DOI10.1021/bi9008825
Alternate JournalBiochemistry
PubMed ID19537707
PubMed Central IDPMC2996727
Grant ListP30 ES000267-34 / ES / NIEHS NIH HHS / United States
P30ES000267 / ES / NIEHS NIH HHS / United States
R01 GM030910 / GM / NIGMS NIH HHS / United States
R01 GM030910-27 / GM / NIGMS NIH HHS / United States
T32 GM008320 / GM / NIGMS NIH HHS / United States
T32 GM065086-07 / GM / NIGMS NIH HHS / United States