Purification, characterization and crystallization of ERA, an essential GTPase from Escherichia coli 1

FEBS Letters

Chen, Su-Min¹  Chen, Xin²  Court, Donald L¹  Ji, Xinhua²  S. Powell, Bradford¹ 

[1] Molecular Control and Genetics Section, ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, P.O. Box B, Frederick, MD 21702, USA;Biomolecular Structure Group, ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, P.O. Box B, Frederick, MD 21702, USA

关键词: ERA;    GTPase;    Purification;    Crystallization;    Escherichia coli;   

DOI  :  10.1016/S0014-5793(99)00178-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown