1JR8

Crystal Structure of Erv2p

1JR8 の概要

• エントリーDOI: 10.2210/pdb1jr8/pdb
• 分子名称: Erv2 PROTEIN, mitochondrial, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: fad, sulfhydryl oxidase, helical bundle, cxxc, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Endoplasmic reticulum membrane; Single-pass type III membrane protein; Lumenal side: Q12284
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28619.81

構造登録者

Gross, E.,Sevier, C.S.,Vala, A.,Kaiser, C.A.,Fass, D. (登録日: 2001-08-13, 公開日: 2001-12-28, 最終更新日: 2024-11-20)

主引用文献

Gross, E.,Sevier, C.S.,Vala, A.,Kaiser, C.A.,Fass, D.
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.
Nat.Struct.Biol., 9:61-67, 2002

PubMed Abstract: Erv2p is an FAD-dependent sulfhydryl oxidase that can promote disulfide bond formation during protein biosynthesis in the yeast endoplasmic reticulum. The structure of Erv2p, determined by X-ray crystallography to 1.5 A resolution, reveals a helix-rich dimer with no global resemblance to other known FAD-binding proteins or thiol oxidoreductases. Two pairs of cysteine residues are required for Erv2p activity. The first (Cys-Gly-Glu-Cys) is adjacent to the isoalloxazine ring of the FAD. The second (Cys-Gly-Cys) is part of a flexible C-terminal segment that can swing into the vicinity of the first cysteine pair in the opposite subunit of the dimer and may shuttle electrons between substrate protein dithiols and the FAD-proximal disulfide.

PubMed: 11740506
DOI: 10.1038/nsb740

実験手法

X-RAY DIFFRACTION (1.5 Å)