Tsuge Hideaki, Tsurumura Toshiharu
Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, 603-8555, Japan,
Curr Top Microbiol Immunol. 2015;384:69-87. doi: 10.1007/82_2014_415.
Mono-ADP-ribosylation is a post-translational protein modification catalyzed by bacterial toxins and exoenzymes that function as ADP-ribosyltransferases. Despite the importance of this modification, the reaction mechanism remains poorly understood due to a lack of information on the crystal structure of these enzymes in complex with a substrate protein. Recently, the structures of two such complexes became available, which shed new light on the mechanisms of mono-ADP-ribosylation. In this review, we consider the reaction mechanism based on the structures of ADP-ribosyltransferases in complex with a substrate protein.
单（ADP-核糖）基化是一种蛋白质翻译后修饰，由作为ADP-核糖基转移酶发挥作用的细菌毒素和外切酶催化。尽管这种修饰很重要，但由于缺乏关于这些酶与底物蛋白复合物晶体结构的信息，其反应机制仍知之甚少。最近，两种此类复合物的结构得以解析，为单（ADP-核糖）基化机制提供了新的线索。在本综述中，我们基于ADP-核糖基转移酶与底物蛋白复合物的结构来探讨反应机制。
