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
1996
Structure of Taq polymerase with DNA at the polymerase active site
Eom S, Wang J, Steitz T. Structure of Taq polymerase with DNA at the polymerase active site. Nature 1996, 382: 278-281. PMID: 8717047, DOI: 10.1038/382278a0.Peer-Reviewed Original ResearchConceptsDuplex DNADNA polymeraseEnded duplex DNAKlenow fragmentBlunt-end terminiActive-site cleftEscherichia coli DNA polymerase IProtein side chainsDNA polymerase ICo-crystal structurePolymerase active siteTaq polymeraseWide minor groovePol ICommon binding sitePolymerase IPolymerase domainExonuclease domainPolymerase cleftThermus aquaticusPolymeraseDNAPolymerase siteMinor grooveExonuclease siteCrystal Structures of an NH2-Terminal Fragment of T4 DNA Polymerase and Its Complexes with Single-Stranded DNA and with Divalent Metal Ions †
Wang J, Yu P, Lin T, Konigsberg W, Steitz T. Crystal Structures of an NH2-Terminal Fragment of T4 DNA Polymerase and Its Complexes with Single-Stranded DNA and with Divalent Metal Ions †. Biochemistry 1996, 35: 8110-8119. PMID: 8679562, DOI: 10.1021/bi960178r.Peer-Reviewed Original ResearchConceptsT4 DNA polymeraseDNA polymeraseExonuclease domainKlenow fragmentExonuclease active siteActive site regionCrystallographic R-factorTranslational regulationMinimal sequence identityMetal ion cofactorsSequence identityActive siteNH2-terminal fragmentNH2-terminalSite regionDivalent metal ion cofactorCarboxylate residuesPolymeraseIon cofactorScissile phosphateEquivalent positionsResidue formsProteinSeparate domainsCrystal structure