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http://purl.uniprot.org/citations/3308869http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3308869http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3308869http://www.w3.org/2000/01/rdf-schema#comment"A single amino acid substitution (Asp to Asn) at position 138 of Escherichia coli elongation factor Tu (EF-Tu) was introduced in the tufA gene clone by oligonucleotide site-directed mutagenesis. The mutated tufA gene was then expressed in maxicells. The properties of [35S]methionine-labeled mutant and wild type EF-Tu were compared by in vitro assays. The Asn-138 mutation greatly reduced the protein's affinity for GDP; however, this mutation dramatically increased the protein's affinity for xanthosine 5'-diphosphate. The mutant protein forms a stable complex with Phe-tRNA and xanthosine 5'-triphosphate, which binds to ribosomes, whereas it does not form a complex with Phe-tRNA and GTP (10 microM). These results suggest that in EF-Tu.nucleoside diphosphate complexes, amino acid residue 138 must interact with the substituent on C-2 of the purine ring. Thus, in wild type EF-Tu, Asp-138 would hydrogen bond to the 2-amino group of GDP, and in the mutant EF-Tu, Asn-138 would form an equivalent hydrogen bond with the 2-carbonyl group of xanthosine 5'-diphosphate. Aspartic acid 138 is conserved in the homologous sequences of all GTP regulatory proteins. This mutation would allow one to specifically alter the nucleotide specificity of other GTP regulatory proteins."xsd:string
http://purl.uniprot.org/citations/3308869http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)45170-8"xsd:string
http://purl.uniprot.org/citations/3308869http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)45170-8"xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/author"Miller D.L."xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/author"Miller D.L."xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/author"Hwang Y.-W."xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/author"Hwang Y.-W."xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/pages"13081-13085"xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/pages"13081-13085"xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/title"A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein."xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/title"A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein."xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/volume"262"xsd:string
http://purl.uniprot.org/citations/3308869http://purl.uniprot.org/core/volume"262"xsd:string
http://purl.uniprot.org/citations/3308869http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3308869
http://purl.uniprot.org/citations/3308869http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3308869
http://purl.uniprot.org/citations/3308869http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3308869
http://purl.uniprot.org/citations/3308869http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3308869
http://purl.uniprot.org/uniprot/P0CE48http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3308869
http://purl.uniprot.org/uniprot/P0CE47http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3308869