Nelson Jennifer A, Uhlenbeck Olke C
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2205 Tech Drive, Hogan 2-100, Evanston, Illinois 60208, USA.
Mol Cell. 2006 Aug;23(4):447-50. doi: 10.1016/j.molcel.2006.08.001.
The recent X-ray crystal structure of a hammerhead ribozyme derived from Schistosoma mansoni containing the rate-enhancing peripheral domain has a catalytic core that is very different from the catalytic core present in the structure of the "minimal" hammerhead, which lacks a peripheral domain (Martick and Scott, 2006). The new structure reconciles many of the disagreements between the minimal hammerhead structure and the biochemical data on the cleavage properties of chemically modified hammerheads. The new structure also emphasizes the dynamic nature of small RNA domains and provides a cautionary tale for everyone who tries to use structure to understand function.
最近,源自曼氏血吸虫的含有速率增强外周结构域的锤头状核酶的X射线晶体结构显示,其催化核心与“最小化”锤头状核酶结构中的催化核心有很大不同,后者缺乏外周结构域(马蒂克和斯科特,2006年)。新结构调和了最小化锤头状核酶结构与化学修饰锤头状核酶切割特性的生化数据之间的许多分歧。新结构还强调了小RNA结构域的动态性质,并为每个试图利用结构来理解功能的人提供了一个警示故事。