Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution

Sylvie Doublié, Stanley Tabor, Alexander M. Long, Charles C. Richardson, Tom Ellenberger

Research output: Contribution to journalArticle

1033 Scopus citations

Abstract

DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10- 6 to 10-6. Here we present a 2.2 Å crystal structure of the replicative DNA polymerase from bacteriophage T7 complexed with a primer-template and a nucleoside triphosphate in the polymeraae active site. The structure illustrate how nucleotides are selected in a template-directed manner, and provides a structural baals for a metal-assisted mechanism of phosphoryl transfer by a large group of related polymerases.

Original languageEnglish
Pages (from-to)251-258
Number of pages8
JournalNature
Volume391
Issue number6664
DOIs
StatePublished - Jan 15 1998

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    Doublié, S., Tabor, S., Long, A. M., Richardson, C. C., & Ellenberger, T. (1998). Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature, 391(6664), 251-258. https://doi.org/10.1038/34593