2003
The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases
Kamtekar S, Kennedy WD, Wang J, Stathopoulos C, Söll D, Steitz TA. The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 1673-1678. PMID: 12578991, PMCID: PMC149891, DOI: 10.1073/pnas.0437911100.Peer-Reviewed Original ResearchConceptsLigand-free conformationCognate amino acidAmino acidsRecent biochemical experimentsProlyl-tRNA synthetasesCysteinyl-tRNA synthetaseProlyl-tRNA synthetaseActive site pocketMethanocaldococcus jannaschiiMethanopyrus kandleriMethanothermobacter thermautotrophicusCognate tRNAEssential enzymeApo formStructural basisBiochemical experimentsAminoacyl-adenylate analoguesHomology modelingConformational changesProtein synthesisTRNAProRSAdenylate complexNanomolar affinitySynthetase
1999
Insights into Editing from an Ile-tRNA Synthetase Structure with tRNAIle and Mupirocin
Silvian L, Wang J, Steitz T. Insights into Editing from an Ile-tRNA Synthetase Structure with tRNAIle and Mupirocin. Science 1999, 285: 1074-1077. PMID: 10446055, DOI: 10.1126/science.285.5430.1074.Peer-Reviewed Original ResearchAcylationAdenosine MonophosphateAmino AcidsBinding SitesCrystallography, X-RayDNA-Directed DNA PolymeraseGlutamate-tRNA LigaseIsoleucineIsoleucine-tRNA LigaseModels, MolecularMupirocinNucleic Acid ConformationOligopeptidesProtein ConformationProtein Structure, SecondaryRNA, Transfer, GlnRNA, Transfer, IleStaphylococcus aureusSubstrate Specificity