Cloning, expression, purification and preliminary X‐ray diffraction studies of a novel AB5 toxin. Issue 8 (31st July 2013)

• Record Type: Journal Article
• Authors: Ng, Natasha; Littler, Dene; Le Nours, Jérôme; Paton, Adrienne W.; Paton, James C.; Rossjohn, Jamie; Beddoe, Travis
• Is Part Of: Acta crystallographica. Volume 69:Issue 8(2013:Aug.)
• Page Start: 912
• Page End: 915
• Publication Date: 2013-07-31
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113018927
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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‐<italic>N</italic>‐glycosidase, ADP‐ribosyltransferase or serine protease activity. However, it has been suggested that a novel AB₅ toxin produced by clinical isolates of <italic>Escherichia coli</italic> and <italic>Citrobacter freundii</italic> has an A subunit with metalloproteinase activity. Here, the expression, purification and crystallization of this novel AB₅ toxin from <italic>E. coli</italic> (EcxAB) and the collection of X‐ray data to 1.9 Å resolution are reported.</p> </abstract>