Article
A partially functional DNA helicase II mutant defective in forming stable binary complexes with ATP and DNA. A role for helicase motif III.
The Journal of biological chemistry - 11 Oct 1996
Brosh R M, Matson S W
Abstract excerpt
To address the functional significance of motif III in Escherichia coli DNA helicase II, the conserved aspartic acid at position 248 was changed to asparagine. UvrDD248N failed to form stable binary complexes with either DNA or ATP. However, UvrDD248N was capable of forming an active ternary comp...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Alleles
- Amino Acid Sequence
- Asparagine
- Aspartic Acid
- Binding Sites
- DNA
- DNA Helicases
- DNA, Viral
- Escherichia coli
- Escherichia coli Proteins
- Kinetics
- Mutagenesis, Site-Directed
- Peptide Fragments
- Recombinant Proteins
- Restriction Mapping
- Ultraviolet Rays