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