3WGD

Crystal structure of ERp46 Trx1

3WGD の概要

• エントリーDOI: 10.2210/pdb3wgd/pdb
• 関連するPDBエントリー: 3WGE
• 分子名称: Thioredoxin domain-containing protein 5, PHOSPHATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: pdi family member, thioredoxin domain, protein disulfide isomerase, isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Endoplasmic reticulum lumen (By similarity): Q8NBS9
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 118522.10

構造登録者

Inaba, K.,Suzuki, M.,Kojima, R. (登録日: 2013-08-04, 公開日: 2014-06-25, 最終更新日: 2024-10-09)

主引用文献

Kojima, R.,Okumura, M.,Masui, S.,Kanemura, S.,Inoue, M.,Saiki, M.,Yamaguchi, H.,Hikima, T.,Suzuki, M.,Akiyama, S.,Inaba, K.
Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family
Structure, 22:431-443, 2014

PubMed Abstract: The mammalian endoplasmic reticulum (ER) contains a diverse oxidative protein folding network in which ERp46, a member of the protein disulfide isomerase (PDI) family, serves as an efficient disulfide bond introducer together with Peroxiredoxin-4 (Prx4). We revealed a radically different molecular architecture of ERp46, in which the N-terminal two thioredoxin (Trx) domains with positively charged patches near their peptide-binding site and the C-terminal Trx are linked by unusually long loops and arranged extendedly, forming an opened V-shape. Whereas PDI catalyzes native disulfide bond formation by the cooperative action of two mutually facing redox-active sites on folding intermediates bound to the central cleft, ERp46 Trx domains are separated, act independently, and engage in rapid but promiscuous disulfide bond formation during early oxidative protein folding. Thus, multiple PDI family members likely contribute to different stages of oxidative folding and work cooperatively to ensure the efficient production of multi-disulfide proteins in the ER.

PubMed: 24462249
DOI: 10.1016/j.str.2013.12.013

実験手法

X-RAY DIFFRACTION (2.5 Å)