Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/81689
Citations | ||
Scopus | Web of Science® | Altmetric |
---|---|---|
?
|
?
|
Type: | Journal article |
Title: | EcxAB is a founding member of a new family of metalloprotease AB₅ toxins with a hybrid cholera-like B subunit |
Other Titles: | EcxAB is a founding member of a new family of metalloprotease AB(5) toxins with a hybrid cholera-like B subunit |
Author: | Ng, N. Littler, D. Paton, A. Le Nours, J. Rossjohn, J. Paton, J. Beddoe, T. |
Citation: | Structure, 2013; 21(11):2003-2013 |
Publisher: | Cell Press |
Issue Date: | 2013 |
ISSN: | 0969-2126 1878-4186 |
Statement of Responsibility: | Natasha M. Ng, Dene R. Littler, Adrienne W. Paton, Jérôme Le Nours, Jamie Rossjohn, James C. Paton, and Travis Beddoe |
Abstract: | AB5 toxins are composed of an enzymatic A subunit that disrupts cellular function associated with a pentameric B subunit required for host cell invasion. EcxAB is an AB5 toxin isolated from clinical strains of Escherichia coli classified as part of the cholera family due to B subunit homology. Cholera-group toxins have catalytic ADP-ribosyltransferases as their A subunits, so it was surprising that EcxA did not. We confirmed that EcxAB self-associates as a functional toxin and obtained its structure. EcxAB is a prototypical member of a hybrid AB5 toxin family containing metzincin-type metalloproteases as their active A subunit paired to a cholera-like B subunit. Furthermore, EcxA is distinct from previously characterized proteases and thus founds an AB5-associated metzincin family that we term the toxilysins. EcxAB provides the first observation of conserved B subunit usage across different AB5 toxin families and provides evidence that the intersubunit interface of these toxins is far more permissive than previously supposed. |
Keywords: | CHO Cells Vero Cells Animals Cricetulus Escherichia coli Metalloproteases Polysaccharides Escherichia coli Proteins Protein Subunits Crystallography, X-Ray Binding Sites Catalytic Domain Protein Structure, Quaternary Protein Structure, Secondary Hydrogen Bonding Models, Molecular Cricetinae Chlorocebus aethiops |
Rights: | © 2013 Elsevier Ltd. |
DOI: | 10.1016/j.str.2013.08.024 |
Grant ID: | ARC |
Published version: | http://dx.doi.org/10.1016/j.str.2013.08.024 |
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.