3ED3

Crystal Structure of the Yeast Dithiol/Disulfide Oxidoreductase Mpd1p

3ED3 の概要

• エントリーDOI: 10.2210/pdb3ed3/pdb
• 関連するPDBエントリー: 2B5E
• 分子名称: Protein disulfide-isomerase MPD1, ACETATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: thioredoxin-like domain, cxxc, isomerase, endoplasmic reticulum, glycoprotein, redox-active center
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Endoplasmic reticulum lumen (Potential): Q12404
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69238.24

構造登録者

Vitu, E.,Greenblatt, H.M.,Fass, D. (登録日: 2008-09-02, 公開日: 2008-11-04, 最終更新日: 2024-11-20)

主引用文献

Vitu, E.,Gross, E.,Greenblatt, H.M.,Sevier, C.S.,Kaiser, C.A.,Fass, D.
Yeast Mpd1p reveals the structural diversity of the protein disulfide isomerase family
J.Mol.Biol., 384:631-640, 2008

PubMed Abstract: Oxidoreductases belonging to the protein disulfide isomerase (PDI) family promote proper disulfide bond formation in substrate proteins in the endoplasmic reticulum. In plants and metazoans, new family members continue to be identified and assigned to various functional niches. PDI-like proteins typically contain tandem thioredoxin-fold domains. The limited information available suggested that the relative orientations of these domains may be quite uniform across the family, and structural models based on this assumption are appearing. However, the X-ray crystal structure of the yeast PDI family protein Mpd1p, described here, demonstrates the radically different domain orientations and surface properties achievable with multiple copies of the thioredoxin fold. A comparison of Mpd1p with yeast Pdi1p expands our perspective on the contexts in which redox-active motifs are presented in the PDI family.

PubMed: 18845159
DOI: 10.1016/j.jmb.2008.09.052

実験手法

X-RAY DIFFRACTION (2 Å)