Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/80030
Citations | ||
Scopus | Web of Science® | Altmetric |
---|---|---|
?
|
?
|
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 |
DOI: | 10.1107/S1744309113018927 |
Grant ID: | ARC |
Published version: | http://dx.doi.org/10.1107/s1744309113018927 |
Appears in Collections: | Aurora harvest 4 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.