Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/80030
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Type: Journal article
Title: Cloning, expression, purification and preliminary X-ray diffraction studies of a novel AB5 toxin
Author: Ng, N.
Littler, D.
Le Nours, J.
Paton, A.
Paton, J.
Rossjohn, J.
Beddoe, T.
Citation: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 2013; 69(8):912-915
Publisher: Blackwell Munksgaard
Issue Date: 2013
ISSN: 1744-3091
1744-3091
Statement of
Responsibility: 
Natasha Ng, Dene Littler, Jérôme Le Nours, Adrienne W. Paton, James C. Paton, Jamie Rossjohn and Travis Beddoe
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.
Keywords: AB5 toxins; Escherichia coli; co-expression; proteases
Rights: © 2013 International Union of Crystallography All rights reserved
RMID: 0020130566
DOI: 10.1107/S1744309113018927
Appears in Collections:Molecular and Biomedical Science publications

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