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 ionsEucaryotesMischarging of M. barkeri tRNAPyl with alanine and serine in vitro
Li D, Polycarpo C, Ambrogelly A, Söll D. Mischarging of M. barkeri tRNAPyl with alanine and serine in vitro. The FASEB Journal 2006, 20: a503-a503. DOI: 10.1096/fasebj.20.4.a503-c.Peer-Reviewed Original ResearchNon-canonical amino acidsSecondary structureCognate tRNA speciesPyrrolysyl-tRNA synthetaseAminoacyl-tRNA synthetaseSimilar secondary structureBovine mitochondriaTRNA speciesAlanine tRNAAnticodon stemAcceptor stemAmino acidsM. barkeriMethanosarcina barkeriSerRSsPyrrolysineMultiple mutationsVariable loopSynthetaseSerineShorter variable loopsSynthetase systemBarkeriAlanineStem
1993
Specificity in RNA: Protein Interactions; the Recognition of Escherichia Coli Glutamine tRNA
Rogers M, Weygand-Durašević I, Schwob E, Sherman J, Rogers K, Thomann H, Sylvers L, Jahn M, Inokuchi H, Ohtsuka E, Söll D. Specificity in RNA: Protein Interactions; the Recognition of Escherichia Coli Glutamine tRNA. 1993, 47-58. DOI: 10.1007/978-1-4615-2407-6_5.Peer-Reviewed Original ResearchProtein interactionsEscherichia coli glutaminyl-tRNA synthetaseRNA-protein structuresRole of tRNAGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetaseCognate aminoacyl-tRNA synthetaseRecognition of tRNAGenetic codeGlutamine tRNAAccuracy of translationRNA structureTRNABiophysical techniquesProtein synthesisMolecular levelMetabolic functionsAminoacyl-tRNA synthetase systemsCurrent understandingRNASynthetase systemSynthetaseUnusual elementsInteractionVariety