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Cloning, expression, purification and preliminary X-ray diffraction studies of a novel AB? toxin.

ABSTRACT: AB? toxins are key virulence factors found in a range of pathogenic bacteria. AB? 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 AB? toxins either have RNA-N-glycosidase, ADP-ribosyltransferase or serine protease activity. However, it has been suggested that a novel AB? 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 AB? toxin from E. coli (EcxAB) and the collection of X-ray data to 1.9 Å resolution are reported.

SUBMITTER: Ng N

PROVIDER: S-EPMC3729173 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

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Cloning, expression, purification and preliminary X-ray diffraction studies of a novel AB₅ toxin.

Ng Natasha N Littler Dene D Le Nours Jérôme J Paton Adrienne W AW Paton James C JC Rossjohn Jamie J Beddoe Travis T

Acta crystallographica. Section F, Structural biology and crystallization communications 20130727 Pt 8

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 clin ...[more]

PMID: 23908042

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