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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification*
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Bacterial Proteins / metabolism
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Chromatography, Affinity
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Crystallization
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Escherichia coli / enzymology*
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Escherichia coli Proteins*
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GTP Phosphohydrolases / chemistry
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GTP Phosphohydrolases / genetics
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GTP Phosphohydrolases / isolation & purification*
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GTP Phosphohydrolases / metabolism
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GTP-Binding Proteins / chemistry
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GTP-Binding Proteins / genetics
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GTP-Binding Proteins / isolation & purification*
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GTP-Binding Proteins / metabolism
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Gene Expression
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Guanosine Diphosphate / metabolism
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RNA-Binding Proteins*
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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RNA-Binding Proteins
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era protein, E coli
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Guanosine Diphosphate
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GTP Phosphohydrolases
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GTP-Binding Proteins