2RUF

Solution structure of the a' domain of thermophilic fungal protein disulfide (reduced form, 303K)

2RUF の概要

• エントリーDOI: 10.2210/pdb2ruf/pdb
• 関連するPDBエントリー: 2kp1 2kp2
• NMR情報: BMRB: 11562
• 分子名称: Protein disulfide-isomerase (1 entity in total)
• 機能のキーワード: thioredoxin fold, isomerase, disulfide bond, endoplasmic reticulum, redox-active center
• 由来する生物種: Humicola insolens (Soft-rot fungus)
• 細胞内の位置: Endoplasmic reticulum lumen : P55059
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13123.91

構造登録者

Inagaki, K.,Satoh, T.,Kato, K. (登録日: 2014-03-31, 公開日: 2015-05-20, 最終更新日: 2024-05-15)

主引用文献

Inagaki, K.,Satoh, T.,Yagi-Utsumi, M.,Le Gulluche, A.C.,Anzai, T.,Uekusa, Y.,Kamiya, Y.,Kato, K.
Redox-coupled structural changes of the catalytic a' domain of protein disulfide isomerase.
Febs Lett., 589:2690-2694, 2015

PubMed Abstract: Protein disulfide isomerase functions as a folding catalyst in the endoplasmic reticulum. Its b' and a' domains provide substrate-binding sites and undergo a redox-dependent domain rearrangement coupled to an open-closed structural change. Here we determined the first solution structure of the a' domain in its oxidized form and thereby demonstrate that oxidation of the a' domain induces significant conformational changes not only in the vicinity of the active site but also in the distal b'-interfacial segment. Based on these findings, we propose that this conformational transition triggers the domain segregation coupled with the exposure of the hydrophobic surface.

PubMed: 26272828
DOI: 10.1016/j.febslet.2015.07.041

実験手法

SOLUTION NMR