1IDM

3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA

1IDM の概要

• エントリーDOI: 10.2210/pdb1idm/pdb
• 分子名称: 3-ISOPROPYLMALATE DEHYDROGENASE (2 entities in total)
• 機能のキーワード: chimera, oxidoreductase
• 由来する生物種: Thermus thermophilus
• 細胞内の位置: Cytoplasm: P00351
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36471.66

構造登録者

Sakurai, M.,Ohzeki, M.,Moriyama, H.,Sato, M.,Tanaka, N. (登録日: 1995-05-19, 公開日: 1995-09-15, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)