Disulfide relays between and within proteins: the Ero1p structure.
Disulfide relays between and within proteins: the Ero1p structure.
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二硫键在蛋白质之间和内部传递：Ero1p 结构。
DOI：
10.1016/j.tibs.2004.08.002
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发表时间：
2004
影响因子：
13.8
通讯作者：
Bardwell,JamesCA
中科院分区：
文献类型：
--
作者：
Hiniker,Annie;Bardwell,JamesCA
必需的黄酶Ero1p既产生新二硫键，又将这些二硫转移到折叠催化剂蛋白二硫异构酶（PDI）上。最近解决的Ero1p晶体结构，结合之前的生化，遗传和结构数据，为Ero1p完成这些任务的机制提供了见解。对er1p与较小的黄素酶Erv2p的比较突出了这些黄素腺嘌呤二核苷酸（FAD）结合巯基氧化酶共有的重要结构元素，并提出了一些可能与产生二硫键的蛋白质共同的一般主题。
The essential flavoenzyme Ero1p both createsde novodisulfide bonds and transfers these disulfides to the folding catalyst protein disulfide isomerase (PDI). The recently solved crystal structure of Ero1p, in combination with previous biochemical, genetic and structural data, provides insight into the mechanism by which Ero1p accomplishes these tasks. A comparison of Ero1p with the smaller flavoenzyme Erv2p highlights important structural elements that are shared by these flavin adenine dinucleotide (FAD)-binding sulfhydryl oxidases and suggests some general themes that might be common to proteins that generate disulfide bonds.