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

Natasha May-Yoke Ng, Dene Littler, Jerome Le Nours, Adrienne Webster Paton, James C Paton, Jamie Rossjohn, Travis Clarke Beddoe

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5 Citations (Scopus)


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 A resolution are reported.
Original languageEnglish
Pages (from-to)912 - 915
Number of pages4
JournalActa Crystallographica Section F: Structural Biology Communications
Issue number8
Publication statusPublished - 2013

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