5HQP

Crystal structure of the ERp44-peroxiredoxin 4 complex

5HQP の概要

• エントリーDOI: 10.2210/pdb5hqp/pdb
• 関連するPDBエントリー: 2R2J 3TJG 3TKP
• 分子名称: Peroxiredoxin-4, Endoplasmic reticulum resident protein 44 (3 entities in total)
• 機能のキーワード: chaperone, gst fold, oxidoreductase, beta/alpha/beta sandwich, oxidoreductase-chaperone complex, oxidoreductase/chaperone
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cytoplasm : Q13162; Endoplasmic reticulum lumen: Q9BS26
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 144386.11

構造登録者

Yang, K.,Li, D.F.,Wang, X.,Wang, C.C. (登録日: 2016-01-22, 公開日: 2016-10-12, 最終更新日: 2024-10-23)

主引用文献

Yang, K.,Li, D.F.,Wang, X.,Liang, J.,Sitia, R.,Wang, C.C.,Wang, X.
Crystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein Retention.
Structure, 24:1755-1765, 2016

PubMed Abstract: ERp44 controls the localization and transport of diverse proteins in the early secretory pathway. The mechanisms that allow client recognition and the source of the oxidative power for forming intermolecular disulfides are as yet unknown. Here we present the structure of ERp44 bound to a client, peroxiredoxin 4. Our data reveal that ERp44 binds the oxidized form of peroxiredoxin 4 via thiol-disulfide interchange reactions. The structure explains the redox-dependent recognition and characterizes the essential non-covalent interactions at the interface. The ERp44-Prx4 covalent complexes can be reduced by glutathione and protein disulfide isomerase family members in the ER, allowing the two components to recycle. This work provides insights into the mechanisms of thiol-mediated protein retention and indicates the key roles of ERp44 in this biochemical cycle to optimize oxidative folding and redox homeostasis.

PubMed: 27642162
DOI: 10.1016/j.str.2016.08.002

実験手法

X-RAY DIFFRACTION (2.6 Å)