2V6O

Structure of Schistosoma mansoni Thioredoxin-Glutathione Reductase (SmTGR)

2V6O の概要

• エントリーDOI: 10.2210/pdb2v6o/pdb
• 分子名称: THIOREDOXIN GLUTATHIONE REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, TETRAETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: fad, flavoprotein, oxidoreductase, chimeric enzyme, thiol-mediated detoxification pathway, redox-active center
• 由来する生物種: SCHISTOSOMA MANSONI (BLOOD FLUKE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 66525.41

構造登録者

Miele, A.E.,Angelucci, F.,Boumis, G.,Dimastrogiovanni, D.,Bellelli, A.,Brunori, M. (登録日: 2007-07-19, 公開日: 2008-03-04, 最終更新日: 2024-10-23)

主引用文献

Angelucci, F.,Miele, A.E.,Boumis, G.,Dimastrogiovanni, D.,Brunori, M.,Bellelli, A.
Glutathione Reductase and Thioredoxin Reductase at the Crossroad: The Structure of Schistosoma Mansoni Thioredoxin Glutathione Reductase
Proteins, 72:936-, 2008

PubMed Abstract: Thioredoxin glutathione reductase (TGR) is a key flavoenzyme expressed by schistosomes that bridges two detoxification pathways crucial for the parasite survival in the host's organism. In this article we report the crystal structure (at 2.2 A resolution) of TGR from Schistosoma mansoni (SmTGR), deleted in the last two residues. The structure reveals the peculiar architecture of this chimeric enzyme: the small Glutaredoxin (Grx) domain at the N-terminus is joined to the large thioredoxin reductase (TR) one via an extended complementary surface, involving residues not conserved in the Grx superfamily; the TR domain interacts with an identical partner via its C-terminal domain, forming a dimer with a twisted "W" shape. Although lacking the penultimate Selenocysteine residue (Sec), the enzyme is still able to reduce oxidized glutathione. These data update the interpretation of the interdomain communication in TGR enzymes. The possible function of this enzyme in pathogenic parasites is discussed.

PubMed: 18300227
DOI: 10.1002/PROT.21986

実験手法

X-RAY DIFFRACTION (2.2 Å)