Cloning, expression, purification and preliminary X-ray diffraction studies of a novel AB5 toxin.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 69(Pt 8): 912-5, 2013 Aug.
Article
em En
| MEDLINE
| ID: mdl-23908042
ABSTRACT
AB5 toxins are key virulence factors found in a range of pathogenic bacteria. AB5 toxins consist of two components a pentameric B subunit that targets eukaryotic cells by binding to glycans located on the cell surface and a catalytic A subunit that disrupts host cellular function following internalization. To date, the A subunits of AB5 toxins either have RNA-N-glycosidase, ADP-ribosyltransferase or serine protease activity. However, it has been suggested that a novel AB5 toxin produced by clinical isolates of Escherichia coli and Citrobacter freundii has an A subunit with metalloproteinase activity. Here, the expression, purification and crystallization of this novel AB5 toxin from E. coli (EcxAB) and the collection of X-ray data to 1.9 Å resolution are reported.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Toxinas Bacterianas
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Regulação Bacteriana da Expressão Gênica
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Clonagem Molecular
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Proteínas de Escherichia coli
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Austrália