Ng, N., Littler, D., Le Nours, J., Paton, A., Paton, J., Rossjohn, Jamie  ORCID: https://orcid.org/0000-0002-2020-7522 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
|
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: | Schools > Medicine Research Institutes & Centres > 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: | 28 Oct 2022 10:02 |
| URI: | https://orca.cardiff.ac.uk/id/eprint/76471 |
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