2009
U2504 Determines the Species Specificity of the A-Site Cleft Antibiotics: The Structures of Tiamulin, Homoharringtonine, and Bruceantin Bound to the Ribosome
Gürel G, Blaha G, Moore PB, Steitz TA. U2504 Determines the Species Specificity of the A-Site Cleft Antibiotics: The Structures of Tiamulin, Homoharringtonine, and Bruceantin Bound to the Ribosome. Journal Of Molecular Biology 2009, 389: 146-156. PMID: 19362093, PMCID: PMC2682339, DOI: 10.1016/j.jmb.2009.04.005.Peer-Reviewed Original ResearchConceptsSpecies specificityLarge ribosomal subunitPeptidyl transferase centerAmino acid side chainsHaloarcula marismortuiRibosomal subunitAcid side chainsSingle nucleotideNeighboring nucleotidesProtein synthesisRibosomesNucleotidesSide chainsMarismortuiInhibitorsSubunitsSpecificityInteractionComplexesA-siteHomoharringtonine
2005
Gene replacement in Haloarcula marismortui: construction of a strain with two of its three chromosomal rRNA operons deleted
Tu D, Blaha G, Moore PB, Steitz TA. Gene replacement in Haloarcula marismortui: construction of a strain with two of its three chromosomal rRNA operons deleted. Extremophiles 2005, 9: 427-435. PMID: 15970993, DOI: 10.1007/s00792-005-0459-y.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBlotting, SouthernChromosome MappingCrystallography, X-RayDNADNA PrimersElectronsEscherichia coli ProteinsGene DeletionGenetic TechniquesHaloarcula marismortuiModels, ChemicalModels, GeneticModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationOperonPlasmidsReverse Transcriptase Polymerase Chain ReactionRibosomal ProteinsRNA-Binding ProteinsRNA, RibosomalRNA, Ribosomal, 23SRRNA OperonSucroseConceptsRRNA operonsHaloarcula marismortuiChromosomal rRNA operonsLarge ribosomal subunitRibosomal protein L22Wild-type organismsSite-directed mutagenesisAmino acid deletionBacteriorhodopsin geneRrnB operonProtein L22Ribosomal subunitRRNA geneGene replacementOperonWild typeRich mediumAcid deletionSuch mutationsGenesHalobacterium halobiumStructural consequencesMarismortuiAtomic resolutionStrainsStructures of MLSBK Antibiotics Bound to Mutated Large Ribosomal Subunits Provide a Structural Explanation for Resistance
Tu D, Blaha G, Moore PB, Steitz TA. Structures of MLSBK Antibiotics Bound to Mutated Large Ribosomal Subunits Provide a Structural Explanation for Resistance. Cell 2005, 121: 257-270. PMID: 15851032, DOI: 10.1016/j.cell.2005.02.005.Peer-Reviewed Original ResearchConceptsLarge ribosomal subunitRibosomal subunitWild-type subunitsWild-type affinityResidue deletion mutantEubacterial ribosomesLarge subunitDeletion mutantsSubunitsResistance phenotypeStreptogramin AVirginiamycin SStructural explanationMutantsRibosomesA2058GAffinityL22BindsCrystal structurePhenotypeBinding
2004
The contribution of metal ions to the structural stability of the large ribosomal subunit
Klein DJ, Moore PB, Steitz TA. The contribution of metal ions to the structural stability of the large ribosomal subunit. RNA 2004, 10: 1366-1379. PMID: 15317974, PMCID: PMC1370624, DOI: 10.1261/rna.7390804.Peer-Reviewed Original ResearchConceptsLarge ribosomal subunitRibosomal subunitMonovalent cation binding siteNucleotide basesSpecific RNA structuresPeptidyl transferase centerLarge RNA moleculesPhylogenetic kingdomsRibosomal proteinsAppearance of proteinsRRNA structureHaloarcula marismortuiMajor groove sideEvolutionary periodRNA moleculesRNA structureCation binding siteStructural domainsTertiary structureProtein groupsMonovalent cationsBinding sitesRRNAGroove sideSubunits
2003
Structures of Five Antibiotics Bound at the Peptidyl Transferase Center of the Large Ribosomal Subunit
Hansen JL, Moore PB, Steitz TA. Structures of Five Antibiotics Bound at the Peptidyl Transferase Center of the Large Ribosomal Subunit. Journal Of Molecular Biology 2003, 330: 1061-1075. PMID: 12860128, DOI: 10.1016/s0022-2836(03)00668-5.Peer-Reviewed Original ResearchConceptsLarge ribosomal subunitPeptidyl transferase centerHydrophobic creviceRibosomal subunitP sitePeptide exit tunnelExit tunnelHaloarcula marismortuiP-loopPeptide bond formationAminoacyl-tRNAVirginiamycin MConformational changesBlasticidin SAntibiotics bindBindsSubunitsCompetitive inhibitorCrevicesSparsomycinTRNARibosomesMarismortui