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http://purl.uniprot.org/citations/23921389http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23921389http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23921389http://www.w3.org/2000/01/rdf-schema#comment"Pathogenic strains of Escherichia coli produce a number of toxins that belong to the AB5 toxin family, which comprise a catalytic A-subunit that induces cellular dysfunction and a B-pentamer that recognizes host glycans. Although the molecular actions of many of the individual subunits of AB5 toxins are well understood, how they self-associate and the effect of this association on cytotoxicity are poorly understood. Here we have solved the structure of the holo-SubAB toxin that, in contrast to other AB5 toxins whose molecular targets are located in the cytosol, cleaves the endoplasmic reticulum chaperone BiP. SubA interacts with SubB in a similar manner to other AB5 toxins via the A2 helix and a conserved disulfide bond that joins the A1 domain with the A2 helix. The structure revealed that the active site of SubA is not occluded by the B-pentamer, and the B-pentamer does not enhance or inhibit the activity of SubA. Structure-based sequence comparisons with other AB5 toxin family members, combined with extensive mutagenesis studies on SubB, show how the hydrophobic patch on top of the B-pentamer plays a dominant role in binding the A-subunit. The structure of SubAB and the accompanying functional characterization of various mutants of SubAB provide a framework for understanding the important role of the B-pentamer in the assembly and the intracellular trafficking of this AB5 toxin."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m113.462622"xsd:string
http://purl.uniprot.org/citations/23921389http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m113.462622"xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Paton J.C."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Paton J.C."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Rossjohn J."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Rossjohn J."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Beddoe T."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Beddoe T."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Johnson M.D."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Johnson M.D."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Paton A.W."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Paton A.W."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Le Nours J."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Le Nours J."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Byres E."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Byres E."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Herdman B.P."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Herdman B.P."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Troy S."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/author"Troy S."xsd:string
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23921389http://purl.uniprot.org/core/date"2013"xsd:gYear