Peter Moore, PhD
Professor Emeritus of ChemistryCards
Appointments
Chemistry
Primary
Contact Info
About
Titles
Professor Emeritus of Chemistry
Appointments
Education & Training
- Postdoctoral Fellow
- Medical Research Council Laboratory of Molecular Biology, Cambridge, UK (1969)
- Postdoctoral Fellow
- Institut de Biologie Moleculaire, University of Geneva, Switzerland (1967)
- PhD
- Harvard University (1966)
Research
Overview
By protein standards, our understanding of RNA structure and function is primitive because it was technically difficult to determine RNA structures for many years. Consequently, even though the technical problems have been overcome, there are lots of RNAs—many of them recently discovered—for which we do not have structures, and hence cannot fully explain their functional properties. The Moore group studies RNA structure/function using NMR and X-ray crystallography as well as molecular biological techniques. The structures being investigated today include: 1) those that form when box H/ACA snoRNAs interact with the rRNA sequences they target for pseudouridylation; and 2) the ribosomal proteins/mRNA complexes responsible for the autogenous regulation of ribosomal protein synthesis. We are also trying to identify the sources of the species specificity shown by many of the antibiotics that inhibit ribosome activity by binding to highly conserved rRNA sequences, and to determine the three-dimensional structure of the eukaryotic ribosome.
Research at a Glance
Yale Co-Authors
Frequent collaborators of Peter Moore's published research.
Publications Timeline
A big-picture view of Peter Moore's research output by year.
Jimin Wang, PhD
20Publications
2,738Citations
Publications
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 ResearchCitationsAltmetricMeSH Keywords and Concepts
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 ResearchCitationsAltmetricU2504 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 ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsSpecies specificityLarge ribosomal subunitPeptidyl transferase centerAmino acid side chainsHaloarcula marismortuiRibosomal subunitAcid side chainsSingle nucleotideNeighboring nucleotidesProtein synthesisRibosomesNucleotidesSide chainsMarismortuiInhibitorsSubunitsSpecificityInteractionComplexesA-siteHomoharringtonine
2008
Crystal structure of the oxazolidinone antibiotic linezolid bound to the 50S ribosomal subunit.
Ippolito JA, Kanyo ZF, Wang D, Franceschi FJ, Moore PB, Steitz TA, Duffy EM. Crystal structure of the oxazolidinone antibiotic linezolid bound to the 50S ribosomal subunit. Journal Of Medicinal Chemistry 2008, 51: 3353-6. PMID: 18494460, DOI: 10.1021/jm800379d.Peer-Reviewed Original ResearchMutations 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 ResearchCitationsAltmetric
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 ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsPseudouridylation 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 ResearchCitationsMeSH Keywords and ConceptsConceptsS 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 ResearchCitationsAltmetric
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 ResearchCitationsMeSH Keywords and ConceptsMeSH 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 ResearchCitations
News
News
- November 20, 2018
Thomas Steitz, Nobel Laureate for ribosome discoveries, dies at 78
- October 11, 2018
Nobel Laureate Thomas A. Steitz Dies, Mapped the Structure of the Ribosome
- August 01, 2011
Nobelist is elected as a member of world’s oldest scientific society
- April 15, 2010
Biotech after the bust
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Sterling Chemistry Lab
225 Prospect Street
New Haven, CT 06511