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http://purl.uniprot.org/citations/14962393http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14962393http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14962393http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/14962393http://www.w3.org/2000/01/rdf-schema#comment"T4 RNA ligase 2 (Rnl2) exemplifies an RNA ligase family that includes the RNA editing ligases (RELs) of Trypanosoma and Leishmania. The Rnl2/REL enzymes are defined by essential signature residues and a unique C-terminal domain, which we show is essential for sealing of 3'-OH and 5'-PO4 RNA ends by Rnl2, but not for ligase adenylation or phosphodiester bond formation at a preadenylated AppRNA end. The N-terminal segment Rnl2(1-249) of the 334 aa Rnl2 protein comprises an autonomous adenylyltransferase/AppRNA ligase domain. We report the 1.9 A crystal structure of the ligase domain with AMP bound at the active site, which reveals a shared fold, catalytic mechanism, and evolutionary history for RNA ligases, DNA ligases, and mRNA capping enzymes."xsd:string
http://purl.uniprot.org/citations/14962393http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2004.01.011"xsd:string
http://purl.uniprot.org/citations/14962393http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2004.01.011"xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/author"Lima C.D."xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/author"Lima C.D."xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/author"Shuman S."xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/author"Shuman S."xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/author"Ho C.K."xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/author"Ho C.K."xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/author"Wang L.K."xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/author"Wang L.K."xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/pages"327-339"xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/pages"327-339"xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/title"Structure and mechanism of RNA ligase."xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/title"Structure and mechanism of RNA ligase."xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/14962393http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/14962393http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14962393