1T7P

T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN

Summary for 1T7P

• Entry DOI: 10.2210/pdb1t7p/pdb
• Descriptor: DNA (5'-D(P*GP*CP*CP*AP*GP*TP*GP*CP*CP*AP*2DA)-3'), DNA (5'-D(P*CP*CP*TP*TP*GP*GP*CP*AP*CP*TP*GP*GP*C)-3'), DNA-directed DNA polymerase, ... (7 entities in total)
• Functional Keywords: t7 dna polymerase, dna replication, nucleotidyl transferase, thioredoxin, processivity factor, complex (hydrolase-electron transport-dna), transferase-dna complex, transferase/dna
• Biological source: Enterobacteria phage T7 (Bacteriophage T7); More
• Total number of polymer chains: 4
• Total formula weight: 98612.03

Authors

Doublie, S.,Tabor, S.,Long, A.M.,Richardson, C.C.,Ellenberger, T. (deposition date: 1997-09-24, release date: 1998-02-25, Last modification date: 2024-02-14)

Primary citation

Doublie, S.,Tabor, S.,Long, A.M.,Richardson, C.C.,Ellenberger, T.
Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution.
Nature, 391:251-258, 1998

PubMed Abstract: 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.

PubMed: 9440688
DOI: 10.1038/34593

Experimental method

X-RAY DIFFRACTION (2.2 Å)