The crystal structure of the thiocyanate-forming protein from Thlaspi arvense, a kelch protein involved in glucosinolate breakdown
The crystal structure of the thiocyanate-forming protein from Thlaspi arvense, a kelch protein involved in glucosinolate breakdown
复制标题
DOI：
10.1007/s11103-015-0351-9
复制
发表时间：
2015-09-01
影响因子：
5.1
通讯作者：
Wittstock, Ute
中科院分区：
文献类型：
--
作者：
Gumz, Frauke;Krausze, Joern;Wittstock, Ute
含有Kelch重复的蛋白质参与了不同的细胞过程，但只有一小部分植物Kelch蛋白质的功能得到了表征。硫氰酸盐形成蛋白(TFP)是十字花科(Brassicaceae)十字花科(Thlaspi Arvense)植物硫氰酸盐形成蛋白(TFP)的代表蛋白，是一类参与植物专化代谢的海带蛋白。硫代葡萄糖苷酶是十字花科植物硫代葡萄糖苷-芥子苷酶系统的组成部分，它决定了植物组织受到破坏，硫代葡萄糖苷被芥子苷酶降解时所形成的生物活性产物的分布。在这里，我们描述了分辨率为1.4a的TaTFP的晶体结构。
Kelch repeat-containing proteins are involved in diverse cellular processes, but only a small subset of plant kelch proteins has been functionally characterized. Thiocyanate-forming protein (TFP) from field-penny cress, Thlaspi arvense (Brassicaceae), is a representative of specifier proteins, a group of kelch proteins involved in plant specialized metabolism. As components of the glucosinolate-myrosinase system of the Brassicaceae, specifier proteins determine the profile of bioactive products formed when plant tissue is disrupted and glucosinolates are hydrolyzed by myrosinases. Here, we describe the crystal structure of TaTFP at a resolution of 1.4 a"