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http://purl.uniprot.org/citations/16511182http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16511182http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16511182http://www.w3.org/2000/01/rdf-schema#comment"The Thermus thermophilus hypothetical protein TTHA1280 belongs to a family of predicted S-adenosyl-L-methionine (AdoMet) dependent RNA methyltransferases (MTases) present in many bacterial and archaeal species. Inspection of amino-acid sequence motifs common to class I Rossmann-fold-like MTases suggested a specific role as an RNA 5-methyluridine MTase. Selenomethionine (SeMet) labelled and native versions of the protein were expressed, purified and crystallized. Two crystal forms of the SeMet-labelled apoprotein were obtained: SeMet-ApoI and SeMet-ApoII. Cocrystallization of the native protein with S-adenosyl-L-homocysteine (AdoHcy) yielded a third crystal form, Native-AdoHcy. The SeMet-ApoI structure was solved by the multiple anomalous dispersion method and refined at 2.55 A resolution. The SeMet-ApoII and Native-AdoHcy structures were solved by molecular replacement and refined at 1.80 and 2.60 A, respectively. TTHA1280 formed a homodimer in the crystals and in solution. Each subunit folds into a three-domain structure composed of a small N-terminal PUA domain, a central alpha/beta-domain and a C-terminal Rossmann-fold-like MTase domain. The three domains form an overall clamp-like shape, with the putative active site facing a deep cleft. The architecture of the active site is consistent with specific recognition of uridine and catalysis of methyl transfer to the 5-carbon position. The cleft is suitable in size and charge distribution for binding single-stranded RNA."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.org/dc/terms/identifier"doi:10.1107/s1744309105029842"xsd:string
http://purl.uniprot.org/citations/16511182http://purl.org/dc/terms/identifier"doi:10.1107/s1744309105029842"xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Kuramitsu S."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Kuramitsu S."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Murayama K."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Murayama K."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Nakagawa N."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Nakagawa N."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Shirouzu M."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Shirouzu M."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Yokoyama S."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Yokoyama S."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Ebihara A."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Ebihara A."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Pioszak A.A."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/author"Pioszak A.A."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/name"Acta Crystallogr. F Struct. Biol. Commun."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/name"Acta Crystallogr. F Struct. Biol. Commun."xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/pages"867-874"xsd:string
http://purl.uniprot.org/citations/16511182http://purl.uniprot.org/core/pages"867-874"xsd:string