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http://purl.uniprot.org/citations/11964156http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11964156http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11964156http://www.w3.org/2000/01/rdf-schema#comment"We have determined the solution structure of ribosomal protein L18 from Thermus thermophilus. L18 is a 12.5 kDa protein of the large subunit of the ribosome and binds to both 5 S and 23 S rRNA. In the uncomplexed state L18 folds to a mixed alpha/beta globular structure with a long disordered N-terminal region. We compared our high-resolution structure with RNA-complexed L18 from Haloarcula marismortui and T. thermophilus to examine RNA-induced as well as species-dependent structural differences. We also identified T. thermophilus S11 as a structural homologue and found that the structures of the RNA-recognition sites are conserved. Important features, for instance a bulge in the RNA-contacting beta-sheet, are conserved in both proteins. We suggest that the L18 fold recognizes a specific RNA motif and that the resulting RNA-protein-recognition module is tolerant to variations in sequence."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.org/dc/terms/identifier"doi:10.1042/0264-6021:3630553"xsd:string
http://purl.uniprot.org/citations/11964156http://purl.org/dc/terms/identifier"doi:10.1042/0264-6021:3630553"xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Haerd T."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Haerd T."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Garber M.B."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Garber M.B."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Gongadze G.M."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Gongadze G.M."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Berglund H."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Berglund H."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Shcherbakov D.V."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Shcherbakov D.V."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Rak A.V."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Rak A.V."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Woestenenk E.A."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/author"Woestenenk E.A."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/pages"553-561"xsd:string
http://purl.uniprot.org/citations/11964156http://purl.uniprot.org/core/pages"553-561"xsd:string