2013
Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics
Xia S, Wood M, Bradley MJ, De La Cruz EM, Konigsberg WH. Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics. Nucleic Acids Research 2013, 41: 9077-9089. PMID: 23921641, PMCID: PMC3799440, DOI: 10.1093/nar/gkt674.Peer-Reviewed Original ResearchConceptsRB69 DNA polymeraseFörster resonance energy transferDNA polymeraseHigh-resolution X-ray crystallographyResolution X-ray crystallographyHigh mutation rateB-family polConformational dynamicsExonuclease domainState kinetic parametersMutation rateG mutantResonance energy transferX-ray crystallographyM variantPolymerasePrimer terminusHydrophobic cavityActive siteBase selectivitySimilar substitutionSide chainsProfound effectDramatic effectInternal cavity
2007
Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates
Zhang H, Cao W, Zakharova E, Konigsberg W, De La Cruz EM. Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates. Nucleic Acids Research 2007, 35: 6052-6062. PMID: 17766250, PMCID: PMC2094073, DOI: 10.1093/nar/gkm587.Peer-Reviewed Original ResearchConceptsHydroxyl groupsNucleotidyl transfer reactionMinimal kinetic schemeConformational changesDetectable fluorescence changeChemical quenchTransfer reactionsDependent fluorescence enhancementFluorescence enhancementFluorescence quenchingFluorescent probeRapid conformational changesTemplate complexN-positionRate constantsFluorescence changesRapid fluorescenceTernary complexKinetic schemeComplexesTemplating baseDependent conformational changesDp/TTemplateFluorescence