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|EcxAB is a founding member of a new family of metalloprotease AB₅ toxins with a hybrid cholera-like B subunit
|EcxAB is a founding member of a new family of metalloprotease AB(5) toxins with a hybrid cholera-like B subunit
Le Nours, J.
|Structure, 2013; 21(11):2003-2013
|Natasha M. Ng, Dene R. Littler, Adrienne W. Paton, Jérôme Le Nours, Jamie Rossjohn, James C. Paton, and Travis Beddoe
|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.
Escherichia coli Proteins
Protein Structure, Quaternary
Protein Structure, Secondary
|© 2013 Elsevier Ltd.
|Appears in Collections:
|Aurora harvest 4
Molecular and Biomedical Science publications
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