2008
Characterization and evolutionary history of an archaeal kinase involved in selenocysteinyl-tRNA formation
Sherrer RL, O’Donoghue P, Söll D. Characterization and evolutionary history of an archaeal kinase involved in selenocysteinyl-tRNA formation. Nucleic Acids Research 2008, 36: 1247-1259. PMID: 18174226, PMCID: PMC2275090, DOI: 10.1093/nar/gkm1134.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAdenosine TriphosphateAmino Acid SequenceArchaeal ProteinsBinding SitesEvolution, MolecularKineticsMethanococcalesModels, MolecularMutationPhosphotransferasesPhylogenyProtein Structure, TertiaryRNA, Transfer, Amino AcylSequence AlignmentSingle-Strand Specific DNA and RNA EndonucleasesSubstrate SpecificityConceptsATPase active sitePhosphate-binding loopInduced fit mechanismRxxxR motifEvolutionary historyWalker BKinase familyPhylogenetic analysisSep-tRNARelated kinasesPSTKBiochemical characterizationSynthase convertsFit mechanismKinaseATPase activityPlasmodium speciesMotifActive siteSerHigh affinityDecreased activityArchaeaSepSecSSer18
2006
A Molecular Tunnel Required for Cooperation of an Asparaginase and a Glu‐tRNAGln Kinase in Gln‐tRNA Formation
Sheppard K, Feng L, Oshikane H, Nakamura Y, Fukai S, Nureki O, Söll D. A Molecular Tunnel Required for Cooperation of an Asparaginase and a Glu‐tRNAGln Kinase in Gln‐tRNA Formation. The FASEB Journal 2006, 20: a503-a503. DOI: 10.1096/fasebj.20.4.a503-a.Peer-Reviewed Original ResearchGlu-tRNAGlnMolecular tunnelMost prokaryotesCo-crystal structurePresence of ATPGln-tRNAGlnSequence similarityEvolutionary linkHeterodimeric enzymeStructural insightsGatDEGatDEnzyme showEnzymatic analysisKinaseAmide donorCrystal structureActive siteATPGlnGluProkaryotesArchaeaTransamidationTight coupling