Zegers I, Loris R, Dehollander G, Fattah Haikal A, Poortmans F, Steyaert J, Wyns L
Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Belgium.
Nat Struct Biol. 1998 Apr;5(4):280-3. doi: 10.1038/nsb0498-280.
Here we present a time-resolved crystallographic analysis of the hydrolysis of exo (Sp) guanosine 2',3'-cyclophosphorothioate by RNase T1. The use of a slow substrate and fast crystallization methods made it possible to perform the study with conventional data-collection techniques. The results support the idea that the hydrolysis reaction proceeds through a mechanism that is the inverse of the transesterification reaction. In addition, the structures provide an explanation for the differential behavior of RNase T1 towards exo- and endo-cyclic thiophosphates.
在此，我们展示了核糖核酸酶T1对外切（Sp）鸟苷2',3'-环硫代磷酸酯水解的时间分辨晶体学分析。使用缓慢底物和快速结晶方法使得利用传统数据收集技术进行该研究成为可能。结果支持了水解反应通过与酯交换反应相反的机制进行的观点。此外，这些结构为核糖核酸酶T1对外环和内环硫代磷酸酯的不同行为提供了解释。
