1RP4

Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell

1RP4 の概要

• エントリーDOI: 10.2210/pdb1rp4/pdb
• 分子名称: Hypothetical 65.0 kDa protein in COX14-COS3 intergenic region precursor, CADMIUM ION, 1-ETHYL-PYRROLIDINE-2,5-DIONE, ... (5 entities in total)
• 機能のキーワード: flavoenzyme, disulfide bonds, cxxcxxc, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side : Q03103
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46317.26

構造登録者

Gross, E.,Kastner, D.B.,Kaiser, C.A.,Fass, D. (登録日: 2003-12-03, 公開日: 2004-06-08, 最終更新日: 2024-11-20)

主引用文献

Gross, E.,Kastner, D.B.,Kaiser, C.A.,Fass, D.
Structure of ero1p, source of disulfide bonds for oxidative protein folding in the cell.
Cell(Cambridge,Mass.), 117:601-610, 2004

PubMed Abstract: The flavoenzyme Ero1p produces disulfide bonds for oxidative protein folding in the endoplasmic reticulum. Disulfides generated de novo within Ero1p are transferred to protein disulfide isomerase and then to substrate proteins by dithiol-disulfide exchange reactions. Despite this key role of Ero1p, little is known about the mechanism by which this enzyme catalyzes thiol oxidation. Here, we present the X-ray crystallographic structure of Ero1p, which reveals the molecular details of the catalytic center, the role of a CXXCXXC motif, and the spatial relationship between functionally significant cysteines and the bound cofactor. Remarkably, the Ero1p active site closely resembles that of the versatile thiol oxidase module of Erv2p, a protein with no sequence homology to Ero1p. Furthermore, both Ero1p and Erv2p display essential dicysteine motifs on mobile polypeptide segments, suggesting that shuttling electrons to a rigid active site using a flexible strand is a fundamental feature of disulfide-generating flavoenzymes.

PubMed: 15163408
DOI: 10.1016/S0092-8674(04)00418-0

実験手法

X-RAY DIFFRACTION (2.2 Å)