3KIJ

Crystal structure of the human PDI-peroxidase

3KIJ の概要

• エントリーDOI: 10.2210/pdb3kij/pdb
• 分子名称: Probable glutathione peroxidase 8, SULFATE ION (3 entities in total)
• 機能のキーワード: human pdi-peroxidase, glutathione peroxidase, membrane, oxidoreductase, peroxidase, transmembrane
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane ; Single-pass membrane protein : Q8TED1
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 63190.11

構造登録者

Nguyen, D.V.,Ruddock, L.W. (登録日: 2009-11-02, 公開日: 2011-01-12, 最終更新日: 2023-09-06)

主引用文献

Nguyen, V.D.,Saaranen, M.J.,Karala, A.R.,Lappi, A.K.,Wang, L.,Raykhel, I.B.,Alanen, H.I.,Salo, K.E.,Wang, C.C.,Ruddock, L.W.
Two Endoplasmic Reticulum PDI Peroxidases Increase the Efficiency of the Use of Peroxide during Disulfide Bond Formation.
J.Mol.Biol., 406:503-515, 2011

PubMed Abstract: Disulfide bond formation in the endoplasmic reticulum by the sulfhydryl oxidase Ero1 family is thought to be accompanied by the concomitant formation of hydrogen peroxide. Since secretory cells can make substantial amounts of proteins that contain disulfide bonds, the production of this reactive oxygen species could have potentially lethal consequences. Here, we show that two human proteins, GPx7 and GPx8, labeled as secreted glutathione peroxidases, are actually endoplasmic reticulum-resident protein disulfide isomerase peroxidases. In vitro, the addition of GPx7 or GPx8 to a folding protein along with protein disulfide isomerase and peroxide enables the efficient oxidative refolding of a reduced denatured protein. Furthermore, both GPx7 and GPx8 interact with Ero1α in vivo, and GPx7 significantly increases oxygen consumption by Ero1α in vitro. Hence, GPx7 and GPx8 may represent a novel route for the productive use of peroxide produced by Ero1α during disulfide bond formation.

PubMed: 21215271
DOI: 10.1016/j.jmb.2010.12.039

実験手法

X-RAY DIFFRACTION (1.8 Å)