2006
Structure of the unusual seryl‐tRNA synthetase reveals a distinct zinc‐dependent mode of substrate recognition
Bilokapic S, Maier T, Ahel D, Gruic‐Sovulj I, Söll D, Weygand‐Durasevic I, Ban N. Structure of the unusual seryl‐tRNA synthetase reveals a distinct zinc‐dependent mode of substrate recognition. The EMBO Journal 2006, 25: 2498-2509. PMID: 16675947, PMCID: PMC1478180, DOI: 10.1038/sj.emboj.7601129.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceAnimalsArchaeal ProteinsBinding SitesCrystallography, X-RayDimerizationEnzyme ActivationHumansMethanosarcina barkeriModels, MolecularMolecular Sequence DataMolecular StructureProtein Structure, QuaternarySequence AlignmentSequence Homology, Amino AcidSerineSerine-tRNA LigaseSubstrate SpecificityThreonineConceptsSeryl-tRNA synthetaseTRNA-binding domainMinimal sequence similarityResolution crystal structureAmino acid substratesActive site zinc ionSequence similaritySubstrate recognitionSerRSsSerine substrateMotif 1Methanogenic archaeaMutational analysisProtein ligandsEnzymatic activityArchaeaAminoacyl-tRNA synthetase systemsDistinct mechanismsAbsolute requirementRecognition mechanismSynthetase systemSynthetaseIon ligandsZinc ionsEucaryotes
2004
The unusual methanogenic seryl‐tRNA synthetase recognizes tRNASer species from all three kingdoms of life
Bilokapic S, Korencic D, Söll D, Weygand‐Durasevic I. The unusual methanogenic seryl‐tRNA synthetase recognizes tRNASer species from all three kingdoms of life. The FEBS Journal 2004, 271: 694-702. PMID: 14764085, DOI: 10.1111/j.1432-1033.2003.03971.x.Peer-Reviewed Original ResearchMeSH KeywordsAnticodonBase SequenceChromatography, GelDimerizationElectrophoretic Mobility Shift AssayEscherichia coliIsoelectric FocusingMethanococcusMolecular Sequence DataNucleic Acid ConformationProtein BindingRNA, Transfer, Amino AcylRNA, Transfer, SerSerineSerine-tRNA LigaseSubstrate SpecificityTranscription, GeneticYeastsConceptsSeryl-tRNA synthetaseGel mobility shift assaysKingdoms of lifeMobility shift assaysMethanococcus jannaschiiM. maripaludisTRNA recognitionShift assaysTRNARenaturation conditionsGel filtration chromatographyConformation of tRNAComplex formationSpeciesFiltration chromatographySynthetaseDimerizationSerRSsJannaschiiTRNASerIsoacceptorsHomologuesComplementary oligonucleotidesAminoacylationRenaturation
2001
Conserved amino acids near the carboxy terminus of bacterial tyrosyl‐tRNA synthetase are involved in tRNA and Tyr‐AMP binding
Salazar J, Zuñiga R, Lefimil C, Söll D, Orellana O. Conserved amino acids near the carboxy terminus of bacterial tyrosyl‐tRNA synthetase are involved in tRNA and Tyr‐AMP binding. FEBS Letters 2001, 491: 257-260. PMID: 11240138, DOI: 10.1016/s0014-5793(01)02214-1.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine MonophosphateBacterial ProteinsCloning, MolecularConserved SequenceDimerizationEscherichia coliGammaproteobacteriaGene ExpressionGenetic Complementation TestGeobacillus stearothermophilusMutagenesis, Site-DirectedRNA, TransferSequence Homology, Amino AcidStructure-Activity RelationshipTyrosineTyrosine-tRNA LigaseConceptsBacterial tyrosyl-tRNA synthetasesBacterial tyrosyl tRNA synthetaseConserved amino acidsAmino acidsAmino acid identityAmino-terminal regionActive site domainCarboxy-terminal segmentTyrosyl-tRNA synthetasesTyrosyl-tRNA synthetaseAcid identityLargest subfamilyCarboxy terminusSite domainTRNA bindingEnzyme functionTyr-AMPTRNATyrRSResiduesEquivalent roleBindingH306S356K395