5NYN

Crystal structure of the atypical poplar thioredoxin-like2.1 in complex with gluathione

5NYN の概要

• エントリーDOI: 10.2210/pdb5nyn/pdb
• 関連するPDBエントリー: 5NYK 5NYL 5NYM 5NYO
• 分子名称: Thioredoxin-like protein 2.1, GLUTATHIONE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: atypical thioredoxin, disulfide exchange, oxidoreductase
• 由来する生物種: Populus tremula x Populus tremuloides
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14594.16

構造登録者

Chibani, K.,Saul, F.A.,Haouz, A.,Rouhier, N. (登録日: 2017-05-11, 公開日: 2018-02-28, 最終更新日: 2025-04-09)

主引用文献

Chibani, K.,Saul, F.,Didierjean, C.,Rouhier, N.,Haouz, A.
Structural snapshots along the reaction mechanism of the atypical poplar thioredoxin-like2.1.
FEBS Lett., 592:1030-1041, 2018

PubMed Abstract: Plastidial thioredoxin (TRX)-like2.1 proteins are atypical thioredoxins possessing a WCRKC active site signature and using glutathione for recycling. To obtain structural information supporting the peculiar catalytic mechanisms and target proteins of these TRXs, we solved the crystal structures of poplar TRX-like2.1 in oxidized and reduced states and of mutated variants. These structures share similar folding with TRXs exhibiting the canonical WCGPC signature. Moreover, the overall conformation is not altered by reduction of the catalytic disulfide bond or in a C45S/C67S variant that formed a disulfide-bridged dimer possibly mimicking reaction intermediates with target proteins. Modeling of the interaction of TRX-like2.1 with both NADPH- and ferredoxin-thioredoxin reductases (FTR) indicates that the presence of Arg43 and Lys44 residues likely precludes reduction by the plastidial FTR.

PubMed: 29453875
DOI: 10.1002/1873-3468.13009

実験手法

X-RAY DIFFRACTION (1.6 Å)