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 Research
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
2007
The 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
2005
Structures 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
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