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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
Statement of
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; Cercopithecus aethiops; 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
Rights: © 2013 Elsevier Ltd.
RMID: 0020133006
DOI: 10.1016/j.str.2013.08.024
Appears in Collections:Molecular and Biomedical Science publications

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