Infidelity out in the open

Sylvie Doublié

doi:10.1016/j.str.2004.09.002

Infidelity out in the open

Structure. 2004 Oct;12(10):1749-50. doi: 10.1016/j.str.2004.09.002.

Author

Sylvie Doublié¹

Affiliation

¹ Department of Microbiology and Molecular Genetics, The University of Vermont, Burlington, VT 05405, USA.

PMID: 15458623
DOI: 10.1016/j.str.2004.09.002

Abstract

The crystal structures of DNA polymerase beta in complex with two different mispairs (A-C and T-C) reveal that the two bases stack partially, rather than engage in hydrogen bonding with each other (Krahn et al., this issue of Structure). The N-domain of the polymerase, which is closed when the correct nucleotide pairs with the template base, adopts a partially open conformation suboptimal for catalysis.

Publication types

News
Comment

MeSH terms

Base Pair Mismatch*
Base Pairing
Crystallography
DNA / chemistry*
DNA Polymerase beta / chemistry*
Nucleic Acid Conformation
Protein Conformation

Substances

DNA
DNA Polymerase beta