Glutathione transferases are structural and functional outliers in the thioredoxin fold.
Glutathione transferases are structural and functional outliers in the thioredoxin fold.
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DOI：
10.1021/bi901180v
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发表时间：
2009-11-24
期刊：
影响因子：
2.9
通讯作者：
Babbitt, Patricia C.
中科院分区：
文献类型：
--
作者：
Atkinson, Holly J.;Babbitt, Patricia C.
谷胱甘肽转移酶（GST）是一种普遍存在的有毒化合物的清除剂，在结构和功能上属于硫氧还蛋白折叠超家族。GST的基本催化能力是在广泛的小的亲电化合物的亲电中心处催化谷胱甘肽的亲核加成或取代。虽然已经详细研究了特定的GST，但对GST不同分组之间的结构和功能关系知之甚少。通过序列和结构相似性的全局分析，确定了细胞溶质（可溶性）GST的两个主要亚组之间谷胱甘肽结合的变化导致谷胱甘肽活化的不同模式。此外，谷胱甘肽结合细胞质GST和线粒体GST κ之间的收敛功能进行了描述。这些结构和功能的主题的识别有助于阐明一些基本的贡献的硫氧还蛋白折叠的GST催化，并澄清如何可以修改硫氧还蛋白折叠，使新的功能。
Glutathione transferases (GSTs) are ubiquitous scavengers of toxic compounds that fall, structurally and functionally, within the thioredoxin fold suprafamily. The fundamental catalytic capability of GSTs is catalysis of the nucleophilic addition or substitution of glutathione at electrophilic centers in a wide range of small electrophilic compounds. While specific GSTs have been studied in detail, little else is known about the structural and functional relationships between different groupings of GSTs. Through a global analysis of sequence and structural similarity, it was determined that variation in the binding of glutathione between the two major subgroups of cytosolic (soluble) GSTs results in a different mode of glutathione activation. Additionally, the convergent features of glutathione binding between cytosolic GSTs and mitochondrial GST kappa are described. The identification of these structural and functional themes helps to illuminate some of the fundamental contributions of the thioredoxin fold to catalysis in the GSTs and clarify how the thioredoxin fold can be modified to enable new functions.
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