3GX0
Crystal Structure of GSH-dependent Disulfide bond Oxidoreductase
Summary for 3GX0
| Entry DOI | 10.2210/pdb3gx0/pdb |
| Descriptor | GST-like protein yfcG, OXIDIZED GLUTATHIONE DISULFIDE (3 entities in total) |
| Functional Keywords | transferase, glutathione, glutathione disulfide, disulfide bond oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 25158.49 |
| Authors | Ladner, J.E.,Harp, J.M.,Wadington, M.C.,Armstrong, R.N. (deposition date: 2009-04-01, release date: 2009-07-07, Last modification date: 2024-02-21) |
| Primary citation | Wadington, M.C.,Ladner, J.E.,Stourman, N.V.,Harp, J.M.,Armstrong, R.N. Analysis of the structure and function of YfcG from Escherichia coli reveals an efficient and unique disulfide bond reductase. Biochemistry, 48:6559-6561, 2009 Cited by PubMed 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. PubMed: 19537707DOI: 10.1021/bi9008825 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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