2017
Crystal structure of Pistol, a class of self-cleaving ribozyme
Nguyen LA, Wang J, Steitz TA. Crystal structure of Pistol, a class of self-cleaving ribozyme. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 1021-1026. PMID: 28096403, PMCID: PMC5293083, DOI: 10.1073/pnas.1611191114.Peer-Reviewed Original Research
2014
Exploiting large non‐isomorphous differences for phase determination of a G‐segment invertase–DNA complex
Ritacco CJ, Steitz TA, Wang J. Exploiting large non‐isomorphous differences for phase determination of a G‐segment invertase–DNA complex. Acta Crystallographica Section D, Structural Biology 2014, 70: 685-693. PMID: 24598738, PMCID: PMC3949525, DOI: 10.1107/s1399004713032392.Peer-Reviewed Original Research
2012
Structural and mechanistic insights into guanylylation of RNA-splicing ligase RtcB joining RNA between 3′-terminal phosphate and 5′-OH
Englert M, Xia S, Okada C, Nakamura A, Tanavde V, Yao M, Eom SH, Konigsberg WH, Söll D, Wang J. Structural and mechanistic insights into guanylylation of RNA-splicing ligase RtcB joining RNA between 3′-terminal phosphate and 5′-OH. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 15235-15240. PMID: 22949672, PMCID: PMC3458315, DOI: 10.1073/pnas.1213795109.Peer-Reviewed Original ResearchConceptsRNA substratesRNA strandRNA phosphate backboneRNA endExtensive mutagenesisSecond RNA substrateKey residuesLigation pathwayBiochemical experimentsOverall ligationRNA ligaseGuanylylationRtcBMechanistic insightsGTP/Critical rolePhosphate backboneGMPActive siteCyclic phosphateDependent reactionDetailed insightStrandsLigaseMutagenesis
2005
Base Selectivity Is Impaired by Mutants that Perturb Hydrogen Bonding Networks in the RB69 DNA Polymerase Active Site †
Yang G, Wang J, Konigsberg W. Base Selectivity Is Impaired by Mutants that Perturb Hydrogen Bonding Networks in the RB69 DNA Polymerase Active Site †. Biochemistry 2005, 44: 3338-3346. PMID: 15736944, DOI: 10.1021/bi047921x.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionBase Pair MismatchBinding SitesDeoxyadenine NucleotidesDeoxycytosine NucleotidesDeoxyguanine NucleotidesDNA-Directed DNA PolymeraseEnterobacterHydrogen BondingKineticsNucleotidesPhenylalanineSubstrate SpecificityThymine NucleotidesTolueneTyrosineViral ProteinsConceptsRB69 polRapid chemical quenchHydrogen bonding networkSet of mutantsStopped-flow fluorescencePutative conformational changesPhosphoryl transfer reactionsPolymerase active siteRB69 DNA polymeraseDNA polymerase active siteChemical quenchMolecular basisBonding networkNoncomplementary dNTPsMutantsTransfer reactionsExo enzymesState kinetic parametersConformational changesMismatched basesActive siteExo formCrystal structureDNA polymeraseNucleoside triphosphates
2004
Pre-Steady-State Kinetics of RB69 DNA Polymerase and Its Exo Domain Mutants: Effect of pH and Thiophosphoryl Linkages on 3‘−5‘ Exonuclease Activity †
Wang C, Zakharova E, Li J, Joyce C, Wang J, Konigsberg W. Pre-Steady-State Kinetics of RB69 DNA Polymerase and Its Exo Domain Mutants: Effect of pH and Thiophosphoryl Linkages on 3‘−5‘ Exonuclease Activity †. Biochemistry 2004, 43: 3853-3861. PMID: 15049692, DOI: 10.1021/bi0302292.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionBacteriophage T4Base Pair MismatchDNA Polymerase IDNA-Directed DNA PolymeraseEnzyme ActivationExodeoxyribonucleasesGlutamineHydrogen-Ion ConcentrationKineticsMutagenesis, Site-DirectedPhosphatesPhosphorylationProtein Structure, TertiaryRNA EditingSubstrate SpecificityT-PhagesThionucleotidesViral ProteinsConceptsRate-determining stepDivalent metal ionsPH-activity profileB family replicative DNA polymerasesChemical stepMetal ionsSingle-turnover conditionsWild-type enzymeEffects of pHKlenow fragmentB-family DNA polymerasesFamily DNA polymerasesState kineticsDNA polymeraseThree-dimensional structureDomain mutantsExonuclease reactionExonuclease activityPhosphorothioate linkagesPhi29 DNA polymeraseElemental effectsReplicative DNA polymerasesRepair DNA polymerasesExo activityCatalysis
2003
Crystal structure of a transcription factor IIIB core interface ternary complex
Juo ZS, Kassavetis GA, Wang J, Geiduschek EP, Sigler PB. Crystal structure of a transcription factor IIIB core interface ternary complex. Nature 2003, 422: 534-539. PMID: 12660736, DOI: 10.1038/nature01534.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBinding SitesCrystallography, X-RayDNA, FungalFungal ProteinsGenes, FungalHydrogen BondingMacromolecular SubstancesModels, MolecularMolecular Sequence DataNucleic Acid ConformationPromoter Regions, GeneticProtein Structure, TertiaryProtein SubunitsRNA, Small NuclearSaccharomyces cerevisiae ProteinsStatic ElectricitySubstrate SpecificityTATA-Box Binding ProteinTranscription Factor TFIIIBConceptsTranscription factor IIIBGeneral transcription factor TFIIBDomain IIÅ resolution crystal structureTranscription factor TFIIBOpen initiation complexRegion of TBPTFIIB-related factorAmino-terminal halfCarboxy-terminal halfTernary complexResolution crystal structureRegulated transcriptionPromoter DNASequence similarityInitiation complexRNA polymeraseBase pairsBdp1Brf1Essential rolePolymerasePrimary interfaceCrystal structureResidue 435
2001
Structure of the Replicating Complex of a Pol α Family DNA Polymerase
Franklin M, Wang J, Steitz T. Structure of the Replicating Complex of a Pol α Family DNA Polymerase. Cell 2001, 105: 657-667. PMID: 11389835, DOI: 10.1016/s0092-8674(01)00367-1.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCrystallographyDNA Polymerase IDNA PrimersDNA ReplicationGene ExpressionHumansNucleotidesProtein Structure, TertiarySubstrate SpecificityConceptsAlpha familyDNA polymeraseResolution crystal structureTernary complex structureApo-protein structurePrimer-template DNAMinor groove interactionsFamily DNA polymerasesFamily polymerasesRB69 DNA polymerasePol IFidelity mechanismsPrimer 3' terminusPrimer extensionPolymeraseGroove interactionsDNA motionTerminusDNA orientationFamilyDNADegrees rotationCrystal structureComplex structureDTTP
2000
Sulfolobus shibatae CCA-adding enzyme forms a tetramer upon binding two tRNA molecules: a scrunching-shuttling model of CCA specificity1 1Edited by T. Richmond
Li F, Wang J, Steitz T. Sulfolobus shibatae CCA-adding enzyme forms a tetramer upon binding two tRNA molecules: a scrunching-shuttling model of CCA specificity1 1Edited by T. Richmond. Journal Of Molecular Biology 2000, 304: 483-492. PMID: 11090289, DOI: 10.1006/jmbi.2000.4189.Peer-Reviewed Original ResearchConceptsActive siteMulti-angle laser lightSmall-angle X-ray scatteringSize exclusion chromatographyX-ray scatteringFurther dimerizationExclusion chromatographyMoleculesDimeric enzymeC basesOligomerization stateTetramerTransfer RNA moleculesLaser lightTRNA moleculesRNA moleculesMonomersPrimer strandChromatographyEnzymeDimersHigh specificityBindingCCA-adding enzymeDimerization
1999
Insights into Editing from an Ile-tRNA Synthetase Structure with tRNAIle and Mupirocin
Silvian L, Wang J, Steitz T. Insights into Editing from an Ile-tRNA Synthetase Structure with tRNAIle and Mupirocin. Science 1999, 285: 1074-1077. PMID: 10446055, DOI: 10.1126/science.285.5430.1074.Peer-Reviewed Original ResearchAcylationAdenosine MonophosphateAmino AcidsBinding SitesCrystallography, X-RayDNA-Directed DNA PolymeraseGlutamate-tRNA LigaseIsoleucineIsoleucine-tRNA LigaseModels, MolecularMupirocinNucleic Acid ConformationOligopeptidesProtein ConformationProtein Structure, SecondaryRNA, Transfer, GlnRNA, Transfer, IleStaphylococcus aureusSubstrate Specificity