3IDV

Crystal structure of the a0a fragment of ERp72

3IDV の概要

• エントリーDOI: 10.2210/pdb3idv/pdb
• 分子名称: Protein disulfide-isomerase A4, ZINC ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: thioredoxin-like fold, disulfide bond, endoplasmic reticulum, isomerase, redox-active center
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Endoplasmic reticulum lumen: P13667
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27003.58

構造登録者

Kozlov, G.,Gehring, K. (登録日: 2009-07-21, 公開日: 2010-07-07, 最終更新日: 2023-09-06)

主引用文献

Kozlov, G.,Azeroual, S.,Rosenauer, A.,Maattanen, P.,Denisov, A.Y.,Thomas, D.Y.,Gehring, K.
Structure of the Catalytic a(0)a Fragment of the Protein Disulfide Isomerase ERp72.
J.Mol.Biol., 401:618-625, 2010

PubMed Abstract: Protein disulfide isomerases (PDIs) are responsible for catalyzing the proper oxidation and isomerization of disulfide bonds of newly synthesized proteins in the endoplasmic reticulum (ER). The ER contains many different PDI-like proteins. Some, such as PDI, are general enzymes that directly recognize misfolded proteins while others, such as ERp57 and ERp72, have more specialized roles. Here, we report the high-resolution X-ray crystal structure of the N-terminal portion of ERp72 (also known as CaBP2 or PDI A4), which contains two a(0)a catalytic thioredoxin-like domains. The structure shows that the a(0) domain contains an additional N-terminal beta-strand and a different conformation of the beta5-alpha4 loop relative to other thioredoxin-like domains. The structure of the a domain reveals that a conserved arginine residue inserts into the hydrophobic core and makes a salt bridge with a conserved glutamate residue in the vicinity of the catalytic site. A structural model of full-length ERp72 shows that all three catalytic sites roughly face each other and positions the adjacent hydrophobic patches that are likely involved in protein substrate binding.

PubMed: 20600112
DOI: 10.1016/j.jmb.2010.06.045

実験手法

X-RAY DIFFRACTION (1.95 Å)