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Cloning, expression, purification and preliminary X-ray diffraction studies of a novel AB5toxin

Ng, N., Littler, D., Le Nours, J., Paton, A., Paton, J., Rossjohn, Jamie and Beddoe, T. 2013. Cloning, expression, purification and preliminary X-ray diffraction studies of a novel AB5toxin. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 69 (8) , pp. 912-915. 10.1107/S1744309113018927

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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 1.9Å resolution are reported.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Systems Immunity Research Institute (SIURI)
Subjects: R Medicine > R Medicine (General)
R Medicine > RZ Other systems of medicine
Uncontrolled Keywords: Bacterial Toxins; Cloning, Molecular; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Protein Subunits; X-Ray Diffraction
Publisher: Wiley
ISSN: 1744-3091
Last Modified: 04 Jun 2017 08:22
URI: http://orca-mwe.cf.ac.uk/id/eprint/76471

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