| http://purl.uniprot.org/citations/15164065 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15164065 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15164065 | http://www.w3.org/2000/01/rdf-schema#comment | "The tripartite cytolethal distending toxin (CDT) induces cell cycle arrest and apoptosis in eukaryotic cells. The subunits CdtA and CdtC associate with the nuclease CdtB to form a holotoxin that translocates CdtB into the host cell, where it acts as a genotoxin by creating DNA lesions. Here we show that the crystal structure of the holotoxin from Haemophilus ducreyi reveals that CDT consists of an enzyme of the DNase-I family, bound to two ricin-like lectin domains. CdtA, CdtB and CdtC form a ternary complex with three interdependent molecular interfaces, characterized by globular, as well as extensive non-globular, interactions. The lectin subunits form a deeply grooved, highly aromatic surface that we show to be critical for toxicity. The holotoxin possesses a steric block of the CdtB active site by means of a non-globular extension of the CdtC subunit, and we identify putative DNA binding residues in CdtB that are essential for toxin activity."xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.org/dc/terms/identifier | "doi:10.1038/nature02532"xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.org/dc/terms/identifier | "doi:10.1038/nature02532"xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/author | "Hsu Y."xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/author | "Hsu Y."xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/author | "Stebbins C.E."xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/author | "Stebbins C.E."xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/author | "Nesic D."xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/author | "Nesic D."xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/pages | "429-433"xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/pages | "429-433"xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/title | "Assembly and function of a bacterial genotoxin."xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/title | "Assembly and function of a bacterial genotoxin."xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/volume | "429"xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://purl.uniprot.org/core/volume | "429"xsd:string |
| http://purl.uniprot.org/citations/15164065 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15164065 |
| http://purl.uniprot.org/citations/15164065 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15164065 |
| http://purl.uniprot.org/citations/15164065 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15164065 |
| http://purl.uniprot.org/citations/15164065 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15164065 |