Crystal structures of a ddATP‐, ddTTP‐, ddCTP, and ddGTP‐ trapped ternary complex of Klentaq1: Insights into nucleotide incorporation and selectivity

• Published in: Protein science Vol. 10; no. 6; pp. 1225 - 1233
• Main Authors: Li, Ying, Waksman, Gabriel
• Format: Journal Article
• Language: English
• Published: Bristol Cold Spring Harbor Laboratory Press 01.06.2001
• Subjects: Binding Sites; Computer Simulation; crystal structure; Deoxyadenine Nucleotides - chemistry; Deoxycytosine Nucleotides - chemistry; Deoxyguanine Nucleotides - chemistry; Dideoxynucleotides; DNA - chemistry; DNA polymerase; DNA-Directed DNA Polymerase - chemistry; fidelity; Kinetics; Klentaq1; Models, Molecular; Nucleotides - chemistry; Protein Binding; Protein Structure, Secondary; Taq Polymerase - chemistry; Thymine Nucleotides - chemistry

The mechanism by which DNA polymerase I enzymes function has been the subject of extensive biochemical and structural studies. We previously determined the structure of a ternary complex of the large fragment of DNA polymerase I from Thermus aquaticus (Klentaq1) bound to a primer/template DNA and a...