A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
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DOI：
10.1038/nsb740
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发表时间：
2002-01-01
期刊：
影响因子：
--
通讯作者：
Fass, D
中科院分区：
文献类型：
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作者：
Gross, E;Sevier, CS;Fass, D
Erv 2 p是一种FAD依赖性巯基氧化酶，可在酵母内质网中蛋白质生物合成期间促进二硫键形成。Erv 2 p的结构，通过X-射线晶体学确定到1.5埃分辨率，揭示了一个富含螺旋的二聚体，与其他已知的FAD结合蛋白或硫醇氧化还原酶没有全局相似性。Erv 2 p活性需要两对半胱氨酸残基。第一个（Cys-Gly-Glu-Cys）与FAD的异咯嗪环相邻。第二个（Cys-Gly-Cys）是柔性C末端片段的一部分，可以摆动到二聚体相对亚基中的第一个半胱氨酸对附近，并可以在底物蛋白二硫醇和FAD近端二硫化物之间穿梭电子。
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.