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
2008
Mutations Outside the Anisomycin-Binding Site Can Make Ribosomes Drug-Resistant
Blaha G, Gürel G, Schroeder SJ, Moore PB, Steitz TA. Mutations Outside the Anisomycin-Binding Site Can Make Ribosomes Drug-Resistant. Journal Of Molecular Biology 2008, 379: 505-519. PMID: 18455733, PMCID: PMC2442718, DOI: 10.1016/j.jmb.2008.03.075.Peer-Reviewed Original Research
2007
Solution Structure of an rRNA Substrate Bound to the Pseudouridylation Pocket of a Box H/ACA snoRNA
Jin H, Loria JP, Moore PB. Solution Structure of an rRNA Substrate Bound to the Pseudouridylation Pocket of a Box H/ACA snoRNA. Molecular Cell 2007, 26: 205-215. PMID: 17466623, DOI: 10.1016/j.molcel.2007.03.014.Peer-Reviewed Original ResearchConceptsPseudouridylation pocketBox H/ACA small nucleolar ribonucleoproteinsBox H/ACA snoRNAsSubstrate sequenceSmall nucleolar ribonucleoproteinSolution structureInteraction motifsNucleolar ribonucleoproteinSpecific uridinesRNA componentRRNA substrateRRNA sequencesSnoRNAsSequencePocketComplexesPseudouridylationSnoRNPsRibonucleoproteinHJ1RNAMotifInteractsStrandsUridineThe Structures of Antibiotics Bound to the E Site Region of the 50 S Ribosomal Subunit of Haloarcula marismortui: 13-Deoxytedanolide and Girodazole
Schroeder SJ, Blaha G, Tirado-Rives J, Steitz TA, Moore PB. The Structures of Antibiotics Bound to the E Site Region of the 50 S Ribosomal Subunit of Haloarcula marismortui: 13-Deoxytedanolide and Girodazole. Journal Of Molecular Biology 2007, 367: 1471-1479. PMID: 17321546, PMCID: PMC1925262, DOI: 10.1016/j.jmb.2007.01.081.Peer-Reviewed Original ResearchConceptsS ribosomal subunitEubacterial ribosomesEukaryotic ribosomesRibosomal subunitHaloarcula marismortuiE siteProtein synthesisSite regionProtein L28RibosomesConformational changesTRNAExtensive interactionsMarismortuiSubunitsStructure of antibioticsBindsSite componentsNew sitesArchaeaEubacteriaSitesL28Crystal structureL15
2006
The Geometry of the Ribosomal Polypeptide Exit Tunnel
Voss NR, Gerstein M, Steitz TA, Moore PB. The Geometry of the Ribosomal Polypeptide Exit Tunnel. Journal Of Molecular Biology 2006, 360: 893-906. PMID: 16784753, DOI: 10.1016/j.jmb.2006.05.023.Peer-Reviewed Original Research
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 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 deacylated tRNA mimics bound to the E site of the large ribosomal subunit
Schmeing TM, Moore PB, Steitz TA. Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit. RNA 2003, 9: 1345-1352. PMID: 14561884, PMCID: PMC1287056, DOI: 10.1261/rna.5120503.Peer-Reviewed Original ResearchStructures 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 ResearchA pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits
Schmeing TM, Seila AC, Hansen JL, Freeborn B, Soukup JK, Scaringe SA, Strobel SA, Moore PB, Steitz TA. A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits. Nature Structural & Molecular Biology 2002, 9: 225-230. PMID: 11828326, DOI: 10.1038/nsb758.Peer-Reviewed Original Research