The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre
The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre
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DOI：
10.1046/j.1432-1033.2003.03519.x
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发表时间：
2003-04-01
期刊：
影响因子：
--
通讯作者：
Lisowsky, T
中科院分区：
文献类型：
--
作者：
Hofhaus, G;Lee, JE;Lisowsky, T
酵母 Erv1p 是一种普遍存在的 FAD 依赖性巯基氧化酶，位于线粒体的膜间隙中。二聚酶对于细胞的生存至关重要。除了靠近 FAD 的氧化还原活性 CXXC 基序外，Erv1p 还含有两个额外的半胱氨酸对。定点诱变已确定所有三个半胱氨酸对对于正常功能至关重要。 C 端半胱氨酸对具有重要的结构意义，因为它有助于 FAD 结合折叠的正确排列。突变蛋白二聚体形成的变化和独特的颜色变化有利于 N 端半胱氨酸对与伴侣单体的氧化还原中心之间的相互作用。
Yeast Erv1p is a ubiquitous FAD-dependent sulfhydryl oxidase, located in the intermembrane space of mitochondria. The dimeric enzyme is essential for survival of the cell. Besides the redox-active CXXC motif close to the FAD, Erv1p harbours two additional cysteine pairs. Site-directed mutagenesis has identified all three cysteine pairs as essential for normal function. The C-terminal cysteine pair is of structural importance as it contributes to the correct arrangement of the FAD-binding fold. Variations in dimer formation and unique colour changes of mutant proteins argue in favour of an interaction between the N-terminal cysteine pair with the redox centre of the partner monomer.