2000
Ancient Adaptation of the Active Site of Tryptophanyl-tRNA Synthetase for Tryptophan Binding †
Ibba M, Stange-Thomann N, Kitabatake M, Ali K, Söll I, Carter, C, Michael Ibba, and, Söll D. Ancient Adaptation of the Active Site of Tryptophanyl-tRNA Synthetase for Tryptophan Binding †. Biochemistry 2000, 39: 13136-13143. PMID: 11052665, DOI: 10.1021/bi001512t.Peer-Reviewed Original ResearchMeSH KeywordsAcylationAnimalsBacillus subtilisBacterial ProteinsBinding SitesCattleDiphosphatesDNA Mutational AnalysisDNA, BacterialEvolution, MolecularGeobacillus stearothermophilusHumansKineticsMiceMutagenesis, Site-DirectedProtein BindingRabbitsRNA, Transfer, TrpSequence Homology, Amino AcidTryptophanTryptophan-tRNA LigaseTyrosineConceptsAmino acid specificityActive site residuesTyrosyl-tRNA synthetasesTryptophanyl-tRNA synthetaseAncient adaptationAnalogous residuesGlu side chainsTryptophan replacementHomologous positionsSystematic mutationAromatic side chainsTrpRSTryptophan recognitionBacillus stearothermophilusSide chainsTryptophan bindingTyrRSResiduesCommon originCompetitive inhibitorMutationsTrp bindingMechanistic supportCatalytic efficiencyActive site
1994
Connecting Anticodon Recognition with the Active Site of Escherichia coli Glutaminyl-tRNA Synthetase
Weygand-Duraševic I, Rogers M, Söll D. Connecting Anticodon Recognition with the Active Site of Escherichia coli Glutaminyl-tRNA Synthetase. Journal Of Molecular Biology 1994, 240: 111-118. PMID: 8027995, DOI: 10.1006/jmbi.1994.1425.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseAnticodon recognitionMutant enzymesEscherichia coli glutaminyl-tRNA synthetaseOpal suppressor tRNASpecificity constantMutant gene productsWild-type enzymeAmino acid loopExtensive conformational changesActive siteNumber of mutationsSuppressor tRNAGene productsGlnRPathways of communicationSaturation mutagenesisTRNAAcceptor stemAcid loopGenetic selectionConformational changesAnticodonPoor substrateAminoacylation
1993
The recognition of E. coli glutamine tRNA by glutaminyl-tRNA synthetase.
Rogers M, Weygand-Durasević I, Schwob E, Sherman J, Rogers K, Thomann H, Sylvers L, Ohtsuka E, Inokuchi H, Söll D. The recognition of E. coli glutamine tRNA by glutaminyl-tRNA synthetase. Nucleic Acids Symposium Series 1993, 211-3. PMID: 7504247.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetase
1988
Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity.
Uemura H, Conley J, Yamao F, Rogers J, Söll D. Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity. Protein Sequences And Data Analysis 1988, 1: 479-85. PMID: 2464170.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseTRNA bindingEscherichia coli glutaminyl-tRNA synthetaseExtensive homology searchesSingle amino acid replacementSingle amino acid changeRegion of homologyAminoacyl-tRNA synthetasesAmino acid replacementsAminoacyl adenylate formationAmino acids 235Amino acid changesLittle apparent similarityGlnS geneTRNA discriminationHomology searchGene productsAcid replacementsShare regionsDifferent tRNAsShort stretchesGenetic selectionAcid changesAsn changeHomology