1A05

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

Summary for 1A05

• Entry DOI: 10.2210/pdb1a05/pdb
• Descriptor: 3-ISOPROPYLMALATE DEHYDROGENASE, MAGNESIUM ION, 3-ISOPROPYLMALIC ACID, ... (4 entities in total)
• Functional Keywords: oxidoreductase, decarboxylating dehydrogenase, leucine biosynthesis
• Biological source: Acidithiobacillus ferrooxidans
• Cellular location: Cytoplasm: Q56268
• Total number of polymer chains: 2
• Total formula weight: 77411.23

Authors

Imada, K.,Inagaki, K.,Matsunami, H.,Kawaguchi, H.,Tanaka, H.,Tanaka, N.,Namba, K. (deposition date: 1997-12-09, release date: 1998-06-17, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)