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• W1597352920 endingPage "13085" @default.
• W1597352920 startingPage "13081" @default.
• W1597352920 abstract "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." @default.
• W1597352920 created "2016-06-24" @default.
• W1597352920 creator A5064200817 @default.
• W1597352920 creator A5073836666 @default.
• W1597352920 date "1987-09-01" @default.
• W1597352920 modified "2023-09-27" @default.
• W1597352920 title "A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein." @default.
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• W1597352920 doi "https://doi.org/10.1016/s0021-9258(18)45170-8" @default.
• W1597352920 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3308869" @default.
• W1597352920 hasPublicationYear "1987" @default.
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