3GRX

NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES

3GRX の概要

• エントリーDOI: 10.2210/pdb3grx/pdb
• NMR情報: BMRB: 4225
• 分子名称: GLUTAREDOXIN 3, GLUTATHIONE (2 entities in total)
• 機能のキーワード: electron transport, thiol-disulfide oxidoreductase, thioltransferase, thioredoxin superfamily
• 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: 9370.60

構造登録者

Nordstrand, K.,Aslund, F.,Holmgren, A.,Otting, G.,Berndt, K.D. (登録日: 1998-08-17, 公開日: 1999-03-30, 最終更新日: 2025-03-26)

主引用文献

Nordstrand, K.,slund, F.,Holmgren, A.,Otting, G.,Berndt, K.D.
NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism.
J.Mol.Biol., 286:541-552, 1999

PubMed Abstract: Glutaredoxins (Grxs) catalyze reversible oxidation/reduction of protein disulfide groups and glutathione-containing mixed disulfide groups via an active site Grx-glutathione mixed disulfide (Grx-SG) intermediate. The NMR solution structure of the Escherichia coli Grx3 mixed disulfide with glutathione (Grx3-SG) was determined using a C14S mutant which traps this intermediate in the redox reaction. The structure contains a thioredoxin fold, with a well-defined binding site for glutathione which involves two intermolecular backbone-backbone hydrogen bonds forming an antiparallel intermolecular beta-bridge between the protein and glutathione. The solution structure of E. coli Grx3-SG also suggests a binding site for a second glutathione in the reduction of the Grx3-SG intermediate, which is consistent with the specificity of reduction observed in Grxs. Molecular details of the structure in relation to the stability of the intermediate and the activity of Grx3 as a reductant of glutathione mixed disulfide groups are discussed. A comparison of glutathione binding in Grx3-SG and ligand binding in other members of the thioredoxin superfamily is presented, which illustrates the highly conserved intermolecular interactions in this protein family.

PubMed: 9973569
DOI: 10.1006/jmbi.1998.2444

実験手法

SOLUTION NMR