1XA8

Crystal Structure Analysis of Glutathione-dependent formaldehyde-activating enzyme (Gfa)

1XA8 の概要

• エントリーDOI: 10.2210/pdb1xa8/pdb
• 関連するPDBエントリー: 1X6M
• 分子名称: Glutathione-dependent formaldehyde-activating enzyme, ZINC ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: formaldehyde, glutathione, s-s bond, lyase
• 由来する生物種: Paracoccus denitrificans
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 87011.83

構造登録者

Neculai, A.M.,Neculai, D.,Griesinger, C.,Vorholt, J.A.,Becker, S. (登録日: 2004-08-25, 公開日: 2004-11-23, 最終更新日: 2023-10-25)

主引用文献

Neculai, A.M.,Neculai, D.,Griesinger, C.,Vorholt, J.A.,Becker, S.
A dynamic zinc redox switch
J.Biol.Chem., 280:2826-2830, 2005

PubMed Abstract: The crystal structures of glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans, which catalyzes the formation of S-hydroxymethylglutathione from formaldehyde and glutathione, and its complex with glutathione (Gfa-GTT) have been determined. Gfa has a new fold with two zinc-sulfur centers, one that is structural (zinc tetracoordinated) and one catalytic (zinc apparently tricoordinated). In Gfa-GTT, the catalytic zinc is displaced due to disulfide bond formation of glutathione with one of the zinc-coordinating cysteines. Soaking crystals of Gfa-GTT with formaldehyde restores the holoenzyme. Accordingly, the displaced zinc forms a complex by scavenging formaldehyde and glutathione. The activation of formaldehyde and of glutathione in this zinc complex favors the final nucleophilic addition, followed by relocation of zinc in the catalytic site. Therefore, the structures of Gfa and Gfa-GTT draw the critical association between a dynamic zinc redox switch and a nucleophilic addition as a new facet of the redox activity of zinc-sulfur sites.

PubMed: 15548539
DOI: 10.1074/jbc.C400517200

実験手法

X-RAY DIFFRACTION (2.4 Å)