1997
Glutamyl-tRNA sythetase.
Freist W, Gauss D, Söll D, Lapointe J. Glutamyl-tRNA sythetase. Biological Chemistry 1997, 378: 1313-29. PMID: 9426192.Peer-Reviewed Original ResearchConceptsGlutamyl-tRNA synthetaseGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesNegative eubacteriaBacterial glutamyl-tRNA synthetasesATP/PPiHigh molecular mass complexesClass I aminoacyl-tRNA synthetasesCytoplasm of eukaryotesE. coli GlnRSGlutamyl-tRNA synthetasesMolecular mass complexesN-terminal halfC-terminal halfAmino acid residuesDihydrouridine (DHU) armPhylogenetic studiesSpecific amidotransferaseGlutamyl-prolylMass complexesTRNA synthetasesCognate tRNAAcid residuesAcceptor stemSynthetases
1994
Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases.
Frugier M, Söll D, Giegé R, Florentz C. Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases. Biochemistry 1994, 33: 9912-21. PMID: 8060999, DOI: 10.1021/bi00199a013.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetasesIdentity nucleotidesHigh-resolution X-ray structuresAminoacyl-tRNA synthetase complexGlutaminyl-tRNA synthetaseAspartyl-tRNA synthetasesAspartyl-tRNA synthetaseGlutamine identityCognate tRNATRNA structureTRNA moleculesTRNAAminoacylation specificitySynthetase complexSpecific aminoacylationConformational changesSynthetasesEscherichia coliYeastSynthetaseNucleotidesE. coliX-ray structureComplex formationColi
1989
Structure of E. coli Glutaminyl-tRNA Synthetase Complexed with tRNAGln and ATP at 2.8 Å Resolution
Rould M, Perona J, Söll D, Steitz T. Structure of E. coli Glutaminyl-tRNA Synthetase Complexed with tRNAGln and ATP at 2.8 Å Resolution. Science 1989, 246: 1135-1142. PMID: 2479982, DOI: 10.1126/science.2479982.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acyl-tRNA SynthetasesAnticodonBase CompositionBase SequenceBinding SitesBiological EvolutionChemical PhenomenaChemistry, PhysicalCrystallizationEscherichia coliMolecular Sequence DataMolecular StructureNucleic Acid ConformationRNA, BacterialRNA, FungalRNA, Transfer, Amino Acid-SpecificRNA, Transfer, GlnX-Ray DiffractionStructural Basis for Misaminoacylation by Mutant E. coli Glutaminyl-tRNA Synthetase Enzymes
Perona J, Swanson R, Rould M, Steitz T, Söll D. Structural Basis for Misaminoacylation by Mutant E. coli Glutaminyl-tRNA Synthetase Enzymes. Science 1989, 246: 1152-1154. PMID: 2686030, DOI: 10.1126/science.2686030.Peer-Reviewed Original Research
1988
Overproduction and purification of Escherichia coli tRNAGln2 and its use in crystallization of the glutaminyl-tRNA synthetase-tRNAGln complex
Perona J, Swanson R, Steitz T, Söll D. Overproduction and purification of Escherichia coli tRNAGln2 and its use in crystallization of the glutaminyl-tRNA synthetase-tRNAGln complex. Journal Of Molecular Biology 1988, 202: 121-126. PMID: 2459391, DOI: 10.1016/0022-2836(88)90524-4.Peer-Reviewed Original Research