3GX0

Crystal Structure of GSH-dependent Disulfide bond Oxidoreductase

3GX0 の概要

• エントリーDOI: 10.2210/pdb3gx0/pdb
• 分子名称: GST-like protein yfcG, OXIDIZED GLUTATHIONE DISULFIDE (3 entities in total)
• 機能のキーワード: transferase, glutathione, glutathione disulfide, disulfide bond oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25158.49

構造登録者

Ladner, J.E.,Harp, J.M.,Wadington, M.C.,Armstrong, R.N. (登録日: 2009-04-01, 公開日: 2009-07-07, 最終更新日: 2024-02-21)

主引用文献

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

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: 19537707
DOI: 10.1021/bi9008825

実験手法

X-RAY DIFFRACTION (2.3 Å)