2009
RB69 DNA Polymerase Mutants with Expanded Nascent Base-Pair-Binding Pockets Are Highly Efficient but Have Reduced Base Selectivity
Zhang H, Beckman J, Wang J, Konigsberg W. RB69 DNA Polymerase Mutants with Expanded Nascent Base-Pair-Binding Pockets Are Highly Efficient but Have Reduced Base Selectivity. Biochemistry 2009, 48: 6940-6950. PMID: 19522539, PMCID: PMC2847438, DOI: 10.1021/bi900422b.Peer-Reviewed Original ResearchConceptsBase pairsCorrect base pairReplicative DNA polymerasesRB69 polRB69 DNA Polymerase MutantsNascent base pairDouble mutantSingle mutantsTriple mutantNumber of substitutionsWild typeMutantsBacteriophage RB69DNA polymerase mutantsPolymerase mutantsDNA polymeraseBinding pocketsNegative selectionDNA polRapid incorporationCatalytic centerLow incorporation efficiencyG mutationSulfolobus solfataricus Dpo4Base discriminationStructures of RB69 DNA polymerase ternary complexes reveal multiple modes of metal ion coordination to correct incoming dNTPs
Wang M, Konigsberg W, Steitz T, Wang J. Structures of RB69 DNA polymerase ternary complexes reveal multiple modes of metal ion coordination to correct incoming dNTPs. The FASEB Journal 2009, 23: 482.1-482.1. DOI: 10.1096/fasebj.23.1_supplement.482.1.Peer-Reviewed Original Research
2008
Structural basis for base discrimination by RB69 DNA polymerase
Wang M, Klimenko D, Steitz T, Wang J. Structural basis for base discrimination by RB69 DNA polymerase. The FASEB Journal 2008, 22: 593.2-593.2. DOI: 10.1096/fasebj.22.1_supplement.593.2.Peer-Reviewed Original ResearchTriple mutantApo formStructural basisBase pairsDNA polymeraseReplicative DNA polymerasesWild-type enzymeTernary complexTemplating baseHelix PBase selectivityNascent base pairRB69 DNA polymeraseBase discriminationWild-type PolType enzymeMismatched base pairsMutantsPol mutantsRB69 polPolymeraseComplexesS565Y416Pol
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