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http://purl.uniprot.org/citations/11839309http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11839309http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11839309http://www.w3.org/2000/01/rdf-schema#comment"Tyrosyl-DNA phosphodiesterase (Tdp1) catalyzes the hydrolysis of a phosphodiester bond between a tyrosine residue and a DNA 3' phosphate. The enzyme appears to be responsible for repairing the unique protein-DNA linkage that occurs when eukaryotic topoisomerase I becomes stalled on the DNA in the cell. The 1.69 A crystal structure reveals that human Tdp1 is a monomer composed of two similar domains that are related by a pseudo-2-fold axis of symmetry. Each domain contributes conserved histidine, lysine, and asparagine residues to form a single active site. The structure of Tdp1 confirms that the protein has many similarities to the members of the phospholipase D (PLD) superfamily and indicates a similar catalytic mechanism. The structure also suggests how the unusual protein-DNA substrate binds and provides insights about the nature of the substrate in vivo."xsd:string
http://purl.uniprot.org/citations/11839309http://purl.org/dc/terms/identifier"doi:10.1016/s0969-2126(02)00707-4"xsd:string
http://purl.uniprot.org/citations/11839309http://purl.org/dc/terms/identifier"doi:10.1016/s0969-2126(02)00707-4"xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/author"Hol W.G.J."xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/author"Hol W.G.J."xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/author"Davies D.R."xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/author"Davies D.R."xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/author"Champoux J.J."xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/author"Champoux J.J."xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/author"Interthal H."xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/author"Interthal H."xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/pages"237-248"xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/pages"237-248"xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/title"The crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1."xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/title"The crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1."xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/11839309http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/11839309http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11839309
http://purl.uniprot.org/citations/11839309http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11839309