2012
Using a Fluorescent Cytosine Analogue tCo To Probe the Effect of the Y567 to Ala Substitution on the Preinsertion Steps of dNMP Incorporation by RB69 DNA Polymerase
Xia S, Beckman J, Wang J, Konigsberg WH. Using a Fluorescent Cytosine Analogue tCo To Probe the Effect of the Y567 to Ala Substitution on the Preinsertion Steps of dNMP Incorporation by RB69 DNA Polymerase. Biochemistry 2012, 51: 4609-4617. PMID: 22616982, PMCID: PMC3437246, DOI: 10.1021/bi300241m.Peer-Reviewed Original Research
2010
Substitution of Ala for Tyr567 in RB69 DNA Polymerase Allows dAMP and dGMP To Be Inserted opposite Guanidinohydantoin,
Beckman J, Wang M, Blaha G, Wang J, Konigsberg WH. Substitution of Ala for Tyr567 in RB69 DNA Polymerase Allows dAMP and dGMP To Be Inserted opposite Guanidinohydantoin,. Biochemistry 2010, 49: 8554-8563. PMID: 20795733, PMCID: PMC3755731, DOI: 10.1021/bi100913v.Peer-Reviewed Original Research
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
The Activity of Selected RB69 DNA Polymerase Mutants Can Be Restored by Manganese Ions: The Existence of Alternative Metal Ion Ligands Used during the Polymerization Cycle †
Zakharova E, Wang J, Konigsberg W. The Activity of Selected RB69 DNA Polymerase Mutants Can Be Restored by Manganese Ions: The Existence of Alternative Metal Ion Ligands Used during the Polymerization Cycle †. Biochemistry 2004, 43: 6587-6595. PMID: 15157091, DOI: 10.1021/bi049615p.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesDeoxyguanine NucleotidesDNA-Directed DNA PolymeraseIonsKineticsLigandsManganeseModels, MolecularMutationProtein ConformationViral ProteinsConceptsMetal ionsRapid chemical quench techniquesB metal ionsMetal ion ligandsMetal ion dependenceNucleotidyl transfer reactionState kinetic analysisTransfer reactionsIon ligandsActive centersCrystal structureSide chainsManganese ionsCatalytic sitePolymerization cyclesIonsIon dependenceAlternative ligandsRB69 DNA Polymerase MutantsLigandsConformational changesPol complexPhosphoryl transferKinetic analysisComplexes