Article
Secondary and tertiary structural changes in gamma delta resolvase: comparison of the wild-type enzyme, the I110R mutant, and the C-terminal DNA binding domain in solution.
Protein science : a publication of the Protein Society - 1 Jun 1997
Pan B, Deng Z, Liu D, Ghosh S, Mullen G P
Abstract excerpt
gamma delta Resolvase is a site-specific DNA recombinase (M(r) 20.5 kDa) in Escherichia coli that shares homology with a family of bacterial resolvases and invertases. We have characterized the secondary and tertiary structural behavior of the cloned DNA binding domain (DBD) and a dimerization de...
Topics
- Ammonium Sulfate
- Binding Sites
- Chromatography, High Pressure Liquid
- Circular Dichroism
- DNA Nucleotidyltransferases
- DNA-Binding Proteins
- Escherichia coli
- Magnetic Resonance Spectroscopy
- Mutation
- Peptide Fragments
- Pliability
- Protein Structure, Secondary
- Protein Structure, Tertiary