PMID:10094501

Citation	Chen, X, Chen, SM, Powell, BS, Court, DL and Ji, X (1999) Purification, characterization and crystallization of ERA, an essential GTPase from Escherichia coli. FEBS Lett. 445:425-30
Abstract	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.
Links	PubMed
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Chromatography, Affinity; Crystallization; Escherichia coli/enzymology; Escherichia coli Proteins; GTP Phosphohydrolases/chemistry; GTP Phosphohydrolases/genetics; GTP Phosphohydrolases/isolation & purification; GTP Phosphohydrolases/metabolism; GTP-Binding Proteins/chemistry; GTP-Binding Proteins/genetics; GTP-Binding Proteins/isolation & purification; GTP-Binding Proteins/metabolism; Gene Expression; Guanosine Diphosphate/metabolism; RNA-Binding Proteins
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