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.
|Number of pages||8|
|State||Published - Jan 15 1998|