Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution.
DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10(-5) to 10(-6). Here we present a 2.2 A crystal structure of the replicative DNA polymerase from bacteriophage T7 complexed with a primer-template and a nucleoside triphosphate in the polymerase active site. The structure illustrates how nucleotides are selected in a template-directed manner, and provides a structural basis for a metal-assisted mechanism of phosphoryl transfer by a large group of related polymerases.
Doublié
S
S
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Tabor
S
S
Long
A M
AM
Richardson
C C
CC
Ellenberger
T
T
D017123:Bacteriophage T7 / Q000737:chemistry*; D001665:Binding Sites; D004269:DNA, Bacterial / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011487:Protein Conformation
D004269:DNA, Bacterial; D008670:Metals; C034970:bacteriophage T7 induced DNA polymerase; D004259:DNA-Directed DNA Polymerase