Article
The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli.
Protein engineering - 1 Mar 1994
Almo S C, Smith D L, Danishefsky A T, Ringe D
Abstract excerpt
Two refined crystal structures of aspartate aminotransferase from E. coli are reported. The wild type enzyme is in the pyridoxal phosphate (PLP) form and its structure has been determined to 2.4 A resolution, refined to an R-factor of 23.2%. The structure of the Arg292Asp mutant has been determined at 2.8 A resolution, refined to an R-factor of 20.3%. The wild type and mutant crystals are isomorphous and the two...
Topics
- Arginine
- Aspartate Aminotransferases
- Aspartic Acid
- Binding Sites
- Crystallization
- Electrochemistry
- Escherichia coli
- Glutamates
- Glutamic Acid
- Hydrogen Bonding
- Molecular Structure