Article
A mutation at the interface between domains causes rearrangement of domains in 3-isopropylmalate dehydrogenase.
Protein engineering - 1 Jan 1997
Qu C, Akanuma S, Moriyama H, Tanaka N, Oshima T
Abstract excerpt
The structure of a thermostable Ala172Leu mutant, designated A172L, of 3-isopropylmalate dehydrogenase from Thermus thermophilus was determined. The crystal belongs to space group P2(1), with cell parameters a = 55.5 A, b = 88.1 A, c = 72.0 A and beta = 100.9 degrees. There is one dimer in each a...
Topics
- 3-Isopropylmalate Dehydrogenase
- Alcohol Oxidoreductases
- Enzyme Stability
- Molecular Structure
- Mutation
- Protein Conformation
- Protein Engineering
- Protein Structure, Tertiary
- Structure-Activity Relationship
- Thermus thermophilus