Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||Cloning, expression, purification and preliminary X-ray diffraction studies of a novel AB5 toxin|
Le Nours, J.
|Citation:||Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 2013; 69(8):912-915|
|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|
|Appears in Collections:||Molecular and Biomedical Science publications|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.