Article
Highly organized but pliant active site of DNA polymerase beta: compensatory mechanisms in mutant enzymes revealed by dynamics simulations and energy analyses.
Biophysical journal - 1 Jun 2004
Yang Linjing, Beard William A, Wilson Samuel H, Broyde Suse, Schlick Tamar
Abstract excerpt
To link conformational transitions noted for DNA polymerases with kinetic results describing catalytic efficiency and fidelity, we investigate the role of key DNA polymerase beta residues on subdomain motion through simulations of five single-residue mutants: Arg-283-Ala, Tyr-271-Ala, Asp-276-Val, Arg-258-Lys, and Arg-258-Ala. Since a movement toward a closed state was only observed for R258A, we suggest that...
Topics
- Binding Sites
- DNA Polymerase beta
- Escherichia coli
- Hydrogen Bonding
- Models, Molecular
- Mutation
- Nucleotides
- Sequence Homology, Amino Acid