3F3R

Crystal structure of yeast Thioredoxin1-glutathione mixed disulfide complex

3F3R の概要

• エントリーDOI: 10.2210/pdb3f3r/pdb
• 関連するPDBエントリー: 3F3Q
• 分子名称: Thioredoxin-1, GLUTATHIONE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: electron transport, thioredoxin, glutathione, deoxyribonucleotide synthesis, golgi apparatus, membrane, nucleus, protein transport, redox-active center, phosphoprotein, transport
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Cytoplasm: P22217
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25018.33

構造登録者

Zhang, Y.R.,Bao, R.,Zhou, C.Z.,Chen, Y.X. (登録日: 2008-10-31, 公開日: 2009-10-20, 最終更新日: 2023-11-01)

主引用文献

Bao, R.,Zhang, Y.R.,Lou, X.,Zhou, C.Z.,Chen, Y.X.
Structural and kinetic analysis of Saccharomyces cerevisiae thioredoxin Trx1: implications for the catalytic mechanism of GSSG reduced by the thioredoxin system
Biochim.Biophys.Acta, 1794:1218-1223, 2009

PubMed Abstract: Thioredoxin (Trx) and glutathione/glutaredoxin (GSH/Grx) systems play the dominant role in cellular redox homeostasis. Recently the Trx system has been shown to be responsible to control the balance of GSH/GSSG once the glutathione reductase system is not available. To decipher the structural basis of electron transfer from the Trx system to GSSG, we solved the crystal structures of oxidized Trx1 and glutathionylated Trx1Cys33Ser mutant at 1.76 and 1.80 A, respectively. Comparative structural analysis revealed a key residue Met35 involved in the Trx-GSSG recognition. Subsequent mutagenesis and kinetic studies proved that Met35Arg mutation could alter the apparent K(m) and V(max) values of the reaction. These findings gave us the structural insights into GSSG reduction catalyzed by the Trx system.

PubMed: 19362171
DOI: 10.1016/j.bbapap.2009.04.001

実験手法

X-RAY DIFFRACTION (1.8 Å)