Ng, Natasha M., Littler, Dene R., Paton, Adrienne W., Le Nours, Jérôme, Rossjohn, Jamie ![]() |
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.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Medicine Systems Immunity Research Institute (SIURI) |
Subjects: | R Medicine > R Medicine (General) R Medicine > RZ Other systems of medicine |
Uncontrolled Keywords: | Animals; Binding Sites; Catalytic Domain; Cercopithecus aethiops; CHO Cells; Cricetinae; Cricetulus; Crystallography X-Ray; Escherichia coli; Escherichia coli Proteins; Hydrogen Bonding; Metalloproteases; Models Molecular; Polysaccharides; Protein Structure Quaternary; Protein Structure Secondary; Protein Subunits; Vero Cells |
Publisher: | Elsevier |
ISSN: | 0969-2126 |
Last Modified: | 28 Oct 2022 09:41 |
URI: | https://orca.cardiff.ac.uk/id/eprint/75369 |
Citation Data
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