title: Purification, characterization and crystallization of ERA, an essential GTPase from Escherichia coli.
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.
authors: Biomolecular Structure Group, ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, MD 21702, USA.
authors: X
authors: X
authors: Chen
authors: S M
authors: SM
authors: Chen
authors: B S
authors: BS
authors: Powell
authors: D L
authors: DL
authors: Court
authors: X
authors: X
authors: Ji
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D015870:Gene Expression; D006153:Guanosine Diphosphate / Q000378:metabolism; D016601:RNA-Binding Proteins
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D016601:RNA-Binding Proteins; C068027:era protein, E coli; D006153:Guanosine Diphosphate; D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins