Chen X, Chen S M, Powell B S, Court D L, Ji X
Biomolecular Structure Group, ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, MD 21702, USA.
FEBS Lett. 1999 Feb 26;445(2-3):425-30. doi: 10.1016/s0014-5793(99)00178-7.
ERA is an essential GTPase widely conserved in bacteria. Homologues of ERA are also present in higher eukaryotic cells. ERA is involved in bacterial cell cycle control at a point preceding cell division. In order to aid the functional investigation of ERA and to facilitate structure-function studies, we have undertaken the X-ray crystallographic analysis of this protein. Here, we report the purification and crystallization procedures and results. The purified ERA exhibits nucleotide-binding activity and GTP-hydrolytic activity. ERA is one of the very few multi-domain GTPases crystallized to date.
ERA是一种在细菌中广泛保守的重要GTP酶。ERA的同源物也存在于高等真核细胞中。ERA在细胞分裂前的一个阶段参与细菌细胞周期调控。为了辅助对ERA的功能研究并促进结构-功能研究，我们对该蛋白进行了X射线晶体学分析。在此，我们报告其纯化、结晶过程及结果。纯化后的ERA表现出核苷酸结合活性和GTP水解活性。ERA是迄今为止极少数已结晶的多结构域GTP酶之一。
