1A05

CRYSTAL STRUCTURE OF THE COMPLEX OF 3-ISOPROPYLMALATE DEHYDROGENASE FROM THIOBACILLUS FERROOXIDANS WITH 3-ISOPROPYLMALATE

1A05 の概要

• エントリーDOI: 10.2210/pdb1a05/pdb
• 分子名称: 3-ISOPROPYLMALATE DEHYDROGENASE, MAGNESIUM ION, 3-ISOPROPYLMALIC ACID, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, decarboxylating dehydrogenase, leucine biosynthesis
• 由来する生物種: Acidithiobacillus ferrooxidans
• 細胞内の位置: Cytoplasm: Q56268
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77411.23

構造登録者

Imada, K.,Inagaki, K.,Matsunami, H.,Kawaguchi, H.,Tanaka, H.,Tanaka, N.,Namba, K. (登録日: 1997-12-09, 公開日: 1998-06-17, 最終更新日: 2024-05-22)

主引用文献

Imada, K.,Inagaki, K.,Matsunami, H.,Kawaguchi, H.,Tanaka, H.,Tanaka, N.,Namba, K.
Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the unique substrate-recognition mechanism.
Structure, 6:971-982, 1998

PubMed Abstract: 3-Isopropylmalate dehydrogenase (IPMDH) and isocitrate dehydrogenase (ICDH) belong to a unique family of bifunctional decarboxylating dehydrogenases. Although the ICDH dimer catalyzes its reaction under a closed conformation, known structures of the IPMDH dimer (without substrate) adopt a fully open or a partially closed form. Considering the similarity in the catalytic mechanism, the IPMDH dimer must be in a fully closed conformation during the reaction. A large conformational change should therefore occur upon substrate binding.

PubMed: 9739088
DOI: 10.1016/S0969-2126(98)00099-9

実験手法

X-RAY DIFFRACTION (2 Å)