Download MendeleyStructure of a loop-deleted variant of 3-isopropylmalate dehydrogenase from Thermus thermophilus: an internal reprieve tolerance mechanism.
Sakurai, M., Ohzeki, M., Miyazaki, K., Moriyama, H., Sato, M., Tanaka, N., Oshima, T.(1996) Acta Crystallogr D Biol Crystallogr 52: 124-128
- PubMed: 15299733
- DOI: https://doi.org/10.1107/S0907444995007190
- Primary Citation of Related Structures:
1IDM - PubMed Abstract:
A loop-deleted mutant form of 3-isopropylmalate dehydrogenase from Thermus thermophilus was constructed to investigate the relationship between the flexibility of the structure and the thermostability of the enzyme. The structure of the mutant enzyme was determined by X-ray crystallography and was found to be almost the same as that of the native enzyme with a reduced temperature factor. Although the mutant protein had lost the flexible loop, its function and thermostability had remained unchanged. This phenomenon can be explained by an internal reprieve tolerance mechanism.
Organizational Affiliation:
Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
