2021
Identification of Mg2+ ions next to nucleotides in cryo‐EM maps using electrostatic potential maps
Wang J, Natchiar SK, Moore PB, Klaholz BP. Identification of Mg2+ ions next to nucleotides in cryo‐EM maps using electrostatic potential maps. Acta Crystallographica Section D, Structural Biology 2021, 77: 534-539. PMID: 33825713, PMCID: PMC8025889, DOI: 10.1107/s2059798321001893.Peer-Reviewed Original ResearchMeSH KeywordsCryoelectron MicroscopyCrystallography, X-RayHumansIonsMacromolecular SubstancesModels, MolecularNucleotidesRibosomes
2009
Structures of Triacetyloleandomycin and Mycalamide A Bind to the Large Ribosomal Subunit of Haloarcula marismortui▿
Gürel G, Blaha G, Steitz TA, Moore PB. Structures of Triacetyloleandomycin and Mycalamide A Bind to the Large Ribosomal Subunit of Haloarcula marismortui▿. Antimicrobial Agents And Chemotherapy 2009, 53: 5010-5014. PMID: 19738021, PMCID: PMC2786347, DOI: 10.1128/aac.00817-09.Peer-Reviewed Original ResearchU2504 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, RibosomalRNA, Ribosomal, 23SRNA-Binding ProteinsRRNA 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 resolutionStrainsThe ribosome revealed
Moore PB, Steitz TA. The ribosome revealed. Trends In Biochemical Sciences 2005, 30: 281-283. PMID: 15950868, DOI: 10.1016/j.tibs.2005.04.006.Peer-Reviewed Original Research
2004
The structure of a ribosomal protein S8/spc operon mRNA complex
Merianos HJ, Wang J, Moore PB. The structure of a ribosomal protein S8/spc operon mRNA complex. RNA 2004, 10: 954-964. PMID: 15146079, PMCID: PMC1370587, DOI: 10.1261/rna.7030704.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBinding SitesCrystallography, X-RayEscherichia coliEscherichia coli ProteinsGenes, BacterialLigandsMacromolecular SubstancesModels, MolecularNucleic Acid ConformationOperonProtein BiosynthesisRibosomal ProteinsRNA, BacterialRNA, MessengerSpecies SpecificityStatic ElectricityConceptsSpc operon mRNAOperon mRNARibosomal protein cistronsSmall ribosomal subunitRibosomal initiation complexResolution crystal structureProtein synthesis resultsSpc operonAutogenous regulationTranslational repressionInitiation complexOwn mRNARibosomal subunitS8 bindingSequence differencesCistronInternal sequencesMRNAGenesConformational similarityBindingComplexesRetroregulationRRNAsOperon
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
2002
Structural insights into peptide bond formation
Hansen JL, Schmeing TM, Moore PB, Steitz TA. Structural insights into peptide bond formation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 11670-11675. PMID: 12185246, PMCID: PMC129327, DOI: 10.1073/pnas.172404099.Peer-Reviewed Original ResearchMeSH KeywordsCrystallizationCrystallography, X-RayHaloarculaModels, MolecularPeptidesProtein ConformationConceptsP-site substrateBond formationHydrogen bondsSecond hydrogen bondPeptide bond formationCarbonyl carbonNucleophilic attackProduct analoguesAmino groupsAlpha-amino groupIntermediate analogueSubstrate complexStructural insightsP siteBondsSite substrateOHHaloarcula marismortui 50S ribosomal subunitAnaloguesSubstrateRibosomal subunitPresence of sparsomycinFormationP-loopComplexesThe Structures of Four Macrolide Antibiotics Bound to the Large Ribosomal Subunit
Hansen JL, Ippolito JA, Ban N, Nissen P, Moore PB, Steitz TA. The Structures of Four Macrolide Antibiotics Bound to the Large Ribosomal Subunit. Molecular Cell 2002, 10: 117-128. PMID: 12150912, DOI: 10.1016/s1097-2765(02)00570-1.Peer-Reviewed Original Research