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http://purl.uniprot.org/citations/15135053http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15135053http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15135053http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/15135053http://www.w3.org/2000/01/rdf-schema#comment"Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine in structural RNA. The pseudouridine synthase TruD, that modifies U13 in tRNA, belongs to a recently identified and large family of pseudouridine synthases present in all kingdoms of life. We report here the crystal structure of Escherichia coli TruD at 2.0 A resolution. The structure reveals an overall V-shaped molecule with an RNA-binding cleft formed between two domains: a catalytic domain and an insertion domain. The catalytic domain has a fold similar to that of the catalytic domains of previously characterised pseudouridine synthases, whereas the insertion domain displays a novel fold."xsd:string
http://purl.uniprot.org/citations/15135053http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2004.03.085"xsd:string
http://purl.uniprot.org/citations/15135053http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2004.03.085"xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/author"Nordlund P."xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/author"Nordlund P."xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/author"Hallberg B.M."xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/author"Hallberg B.M."xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/author"Ericsson U.B."xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/author"Ericsson U.B."xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/pages"59-64"xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/pages"59-64"xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/title"X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold."xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/title"X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold."xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/volume"565"xsd:string
http://purl.uniprot.org/citations/15135053http://purl.uniprot.org/core/volume"565"xsd:string
http://purl.uniprot.org/citations/15135053http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15135053
http://purl.uniprot.org/citations/15135053http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15135053
http://purl.uniprot.org/citations/15135053http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15135053