A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p

被引：134

作者：

Gross, E

Sevier, CS

Vala, A

Kaiser, CA

Fass, D ^{[1
]}

机构：

[1] Weizmann Inst Sci, Dept Struct Chem, IL-76100 Rehovot, Israel

[2] MIT, Dept Biol, Cambridge, MA 02139 USA

来源：

NATURE STRUCTURAL BIOLOGY | 2002年 / 9卷 / 01期

关键词：

D O I：

10.1038/nsb740

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom 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.

引用

页码：61 / 67

页数：7

共 49 条

[41] Calcium-mediated thermostability in the subtilisin superfamily:: The crystal structure of Bacillus Ak.1 protease at 1.8 Å resolution [J].