The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
about
Molecular events during translocation and proofreading extracted from 200 static structures of DNA polymerase.Kinetics of Mismatch Formation opposite Lesions by the Replicative DNA Polymerase from Bacteriophage RB69Substitution of Ala for Tyr567 in RB69 DNA Polymerase Allows dAMP To Be Inserted opposite 7,8-Dihydro-8-oxoguanine,Substitution of Ala for Tyr567 in RB69 DNA Polymerase Allows dAMP and dGMP To Be Inserted opposite Guanidinohydantoin,Insights into Base Selectivity from the 1.8 Å Resolution Structure of an RB69 DNA Polymerase Ternary ComplexVariation in Mutation Rates Caused by RB69pol Fidelity Mutants Can Be Rationalized on the Basis of Their Kinetic Behavior and Crystal StructuresStructural Insights into Complete Metal Ion Coordination from Ternary Complexes of B Family RB69 DNA PolymeraseA strategically located serine residue is critical for the mutator activity of DNA polymerase IV from Escherichia coliUsing a Fluorescent Cytosine Analogue tC o To Probe the Effect of the Y567 to Ala Substitution on the Preinsertion Steps of dNMP Incorporation by RB69 DNA PolymeraseContribution of Partial Charge Interactions and Base Stacking to the Efficiency of Primer Extension at and beyond Abasic Sites in DNAA Remote Palm Domain Residue of RB69 DNA Polymerase Is Critical for Enzyme Activity and Influences the Conformation of the Active SiteRB69 DNA polymerase structure, kinetics, and fidelity.Identification of critical residues for the tight binding of both correct and incorrect nucleotides to human DNA polymerase λReversal of a mutator activity by a nearby fidelity-neutral substitution in the RB69 DNA polymerase binding pocket.Significant contribution of the 3'→5' exonuclease activity to the high fidelity of nucleotide incorporation catalyzed by human DNA polymerase ϵ.The roles of Tyr391 and Tyr619 in RB69 DNA polymerase replication fidelity.Mechanism of inhibition of human immunodeficiency virus type 1 reverse transcriptase by a stavudine analogue, 4'-ethynyl stavudine triphosphateSingle-molecule investigation of substrate binding kinetics and protein conformational dynamics of a B-family replicative DNA polymerase.Utility of the bacteriophage RB69 polymerase gp43 as a surrogate enzyme for herpesvirus orthologs.RB69 DNA polymerase mutants with expanded nascent base-pair-binding pockets are highly efficient but have reduced base selectivity.Effect of Different Divalent Cations on the Kinetics and Fidelity of RB69 DNA Polymerase.Nucleic acid polymerases use a general acid for nucleotidyl transfer.
P2860
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P2860
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
description
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name
The L561A substitution in the ...... e reduces base discrimination.
@ast
The L561A substitution in the ...... e reduces base discrimination.
@en
type
label
The L561A substitution in the ...... e reduces base discrimination.
@ast
The L561A substitution in the ...... e reduces base discrimination.
@en
prefLabel
The L561A substitution in the ...... e reduces base discrimination.
@ast
The L561A substitution in the ...... e reduces base discrimination.
@en
P2093
P2860
P356
P1433
P1476
The L561A substitution in the ...... e reduces base discrimination.
@en
P2093
Chanu Rhee
Hong Zhang
Jimin Wang
John W Drake
William Konigsberg
P2860
P304
P356
10.1021/BI052099Y
P407
P50
P577
2006-02-01T00:00:00Z