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https://hdl.handle.net/2440/81689
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dc.contributor.author | Ng, N. | - |
dc.contributor.author | Littler, D. | - |
dc.contributor.author | Paton, A. | - |
dc.contributor.author | Le Nours, J. | - |
dc.contributor.author | Rossjohn, J. | - |
dc.contributor.author | Paton, J. | - |
dc.contributor.author | Beddoe, T. | - |
dc.date.issued | 2013 | - |
dc.identifier.citation | Structure, 2013; 21(11):2003-2013 | - |
dc.identifier.issn | 0969-2126 | - |
dc.identifier.issn | 1878-4186 | - |
dc.identifier.uri | http://hdl.handle.net/2440/81689 | - |
dc.description.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. | - |
dc.description.statementofresponsibility | Natasha M. Ng, Dene R. Littler, Adrienne W. Paton, Jérôme Le Nours, Jamie Rossjohn, James C. Paton, and Travis Beddoe | - |
dc.language.iso | en | - |
dc.publisher | Cell Press | - |
dc.rights | © 2013 Elsevier Ltd. | - |
dc.source.uri | http://dx.doi.org/10.1016/j.str.2013.08.024 | - |
dc.subject | CHO Cells | - |
dc.subject | Vero Cells | - |
dc.subject | Animals | - |
dc.subject | Cricetulus | - |
dc.subject | Escherichia coli | - |
dc.subject | Metalloproteases | - |
dc.subject | Polysaccharides | - |
dc.subject | Escherichia coli Proteins | - |
dc.subject | Protein Subunits | - |
dc.subject | Crystallography, X-Ray | - |
dc.subject | Binding Sites | - |
dc.subject | Catalytic Domain | - |
dc.subject | Protein Structure, Quaternary | - |
dc.subject | Protein Structure, Secondary | - |
dc.subject | Hydrogen Bonding | - |
dc.subject | Models, Molecular | - |
dc.subject | Cricetinae | - |
dc.subject | Chlorocebus aethiops | - |
dc.title | EcxAB is a founding member of a new family of metalloprotease AB₅ toxins with a hybrid cholera-like B subunit | - |
dc.title.alternative | EcxAB is a founding member of a new family of metalloprotease AB(5) toxins with a hybrid cholera-like B subunit | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1016/j.str.2013.08.024 | - |
dc.relation.grant | ARC | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Paton, J. [0000-0001-9807-5278] | - |
Appears in Collections: | Aurora harvest 4 Molecular and Biomedical Science publications |
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