1IDM

3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA

Summary for 1IDM

• Entry DOI: 10.2210/pdb1idm/pdb
• Descriptor: 3-ISOPROPYLMALATE DEHYDROGENASE (2 entities in total)
• Functional Keywords: chimera, oxidoreductase
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: P00351
• Total number of polymer chains: 1
• Total formula weight: 36471.66

Authors

Sakurai, M.,Ohzeki, M.,Moriyama, H.,Sato, M.,Tanaka, N. (deposition date: 1995-05-19, release date: 1995-09-15, Last modification date: 2024-02-07)

Primary citation

Sakurai, M.,Ohzeki, M.,Miyazaki, K.,Moriyama, H.,Sato, M.,Tanaka, N.,Oshima, T.
Structure of a loop-deleted variant of 3-isopropylmalate dehydrogenase from Thermus thermophilus: an internal reprieve tolerance mechanism.
Acta Crystallogr.,Sect.D, 52:124-128, 1996

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.

PubMed: 15299733
DOI: 10.1107/S0907444995007190

Experimental method

X-RAY DIFFRACTION (2.2 Å)