Loss of DNA polymerase beta stacking interactions with templating purines, but not pyrimidines, alters catalytic efficiency and fidelity.

doi:10.1074/jbc.M107286200

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Article

Loss of DNA polymerase beta stacking interactions with templating purines, but not pyrimidines, alters catalytic efficiency and fidelity.

The Journal of biological chemistry - 8 Mar 2002

Beard William A, Shock David D, Yang Xiao-Ping, DeLauder Saundra F, Wilson Samuel H

Abstract excerpt

Structures of DNA polymerases bound with DNA reveal that the 5'-trajectory of the template strand is dramatically altered as it exits the polymerase active site. This distortion provides the polymerase access to the nascent base pair to interrogate proper Watson-Crick geometry. Upon binding a correct deoxynucleoside triphosphate, alpha-helix N of DNA polymerase beta is observed to form one face of the binding...

Topics

Arginine
Aspartic Acid
Base Pair Mismatch
Binding Sites
Catalysis
DNA
DNA Polymerase beta
Dose-Response Relationship, Drug
Glycine
Humans
Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Kinetics

Lysine

Models, Chemical

Models, Molecular

Mutagenesis, Site-Directed

Mutation

Protein Binding

Source

Open in PubMed

Identifiers

PMID: 11756435
DOI: 10.1074/jbc.M107286200

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