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http://purl.uniprot.org/citations/20430012http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20430012http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20430012http://www.w3.org/2000/01/rdf-schema#comment"In mammalian cells, a family of mitochondrial transcription termination factors (MTERFs) regulates mitochondrial gene expression. MTERF family members share a approximately 270 residues long MTERF-domain required for DNA binding and transcription regulation. However, the structure of this widely conserved domain is unknown. Here, we show that the MTERF-domain of human MTERF3 forms a half-doughnut-shaped right-handed superhelix. The superhelix is built from alpha-helical tandem repeats that display a novel triangular three-helix motif. This repeat motif, which we denote the MTERF-motif, is a conserved structural element present in proteins from metazoans, plants, and protozoans. Furthermore, a narrow, strongly positively charged nucleic acid-binding path is found in the middle of the concave side of the half-doughnut. This arrangement suggests a half clamp nucleic acid-binding mode for MTERF-domains."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2010.04.130"xsd:string
http://purl.uniprot.org/citations/20430012http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2010.04.130"xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/author"Gustafsson C.M."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/author"Gustafsson C.M."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/author"Samuelsson T."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/author"Samuelsson T."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/author"Spaahr H."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/author"Spaahr H."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/author"Haellberg B.M."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/author"Haellberg B.M."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/pages"386-390"xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/pages"386-390"xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/title"Structure of mitochondrial transcription termination factor 3 reveals a novel nucleic acid-binding domain."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/title"Structure of mitochondrial transcription termination factor 3 reveals a novel nucleic acid-binding domain."xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/volume"397"xsd:string
http://purl.uniprot.org/citations/20430012http://purl.uniprot.org/core/volume"397"xsd:string
http://purl.uniprot.org/citations/20430012http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20430012
http://purl.uniprot.org/citations/20430012http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20430012