3APS

Crystal structure of Trx4 domain of ERdj5

3APS の概要

• エントリーDOI: 10.2210/pdb3aps/pdb
• 関連するPDBエントリー: 3APO 3APQ
• 分子名称: DnaJ homolog subfamily C member 10, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: thioredoxin fold, cxxc motif, endoplasmic reticulum, oxidoreductase
• 由来する生物種: Mus musculus (MOUSE)
• 細胞内の位置: Secreted (Potential): Q9DC23
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28074.31

構造登録者

Inaba, K.,Suzuki, M.,Nagata, K. (登録日: 2010-10-20, 公開日: 2011-04-20, 最終更新日: 2024-10-23)

主引用文献

Hagiwara, M.,Maegawa, K.,Suzuki, M.,Ushioda, R.,Araki, K.,Matsumoto, Y.,Hoseki, J.,Nagata, K.,Inaba, K.
Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5.
Mol.Cell, 41:432-444, 2011

PubMed Abstract: ER-associated degradation (ERAD) is an ER quality-control process that eliminates terminally misfolded proteins. ERdj5 was recently discovered to be a key ER-resident PDI family member protein that accelerates ERAD by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. We here solved the crystal structure of full-length ERdj5, thereby revealing that ERdj5 contains the N-terminal J domain and six tandem thioredoxin domains that can be divided into the N- and C-terminal clusters. Our systematic biochemical analyses indicated that two thioredoxin domains that constitute the C-terminal cluster form the highly reducing platform that interacts with EDEM1 and reduces EDEM1-recruited substrates, leading to their facilitated degradation. The pulse-chase experiment further provided direct evidence for the sequential movement of an ERAD substrate from calnexin to the downstream EDEM1-ERdj5 complex, and then to the retrotranslocation channel, probably through BiP. We present a detailed molecular view of how ERdj5 mediates ERAD in concert with EDEM1.

PubMed: 21329881
DOI: 10.1016/j.molcel.2011.01.021

実験手法

X-RAY DIFFRACTION (1.9 Å)