RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/15304566http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15304566http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15304566http://www.w3.org/2000/01/rdf-schema#comment"The bipartite DNA-binding domain of Tc3 transposase, Tc3A, was crystallized in complex with its transposon recognition sequence. In the structure the two DNA-binding domains form structurally related helix-turn-helix (HTH) motifs. They both bind to the major groove on a single DNA oligomer, separated by a linker that interacts closely with the minor groove. The structure resembles that of the transcription factor Pax6 DNA-binding domain, but the relative orientation of the HTH-domain is different. The DNA conformation is distorted, characterized by local narrowing of the minor groove and bends at both ends. The protein-DNA recognition takes place through base and backbone contacts, as well as shape-recognition of the distortions in the DNA. Charged interactions are primarily found in the N-terminal domain and the linker indicating that these may form the initial contact area. Two independent dimer interfaces could be relevant for bringing together transposon ends and for binding to a direct repeat site in the transposon end. In contrast to the Tn5 synaptic complex, the two Tc3A DNA-binding domains bind to a single Tc3 transposon end."xsd:string
http://purl.uniprot.org/citations/15304566http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkh770"xsd:string
http://purl.uniprot.org/citations/15304566http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkh770"xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/author"Sixma T.K."xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/author"Sixma T.K."xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/author"van Pouderoyen G."xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/author"van Pouderoyen G."xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/author"Watkins S."xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/author"Watkins S."xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/pages"4306-4312"xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/pages"4306-4312"xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/title"Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA."xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/title"Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA."xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/volume"32"xsd:string
http://purl.uniprot.org/citations/15304566http://purl.uniprot.org/core/volume"32"xsd:string
http://purl.uniprot.org/citations/15304566http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15304566
http://purl.uniprot.org/citations/15304566http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15304566
http://purl.uniprot.org/citations/15304566http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15304566
http://purl.uniprot.org/citations/15304566http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15304566