1ITW

Crystal structure of the monomeric isocitrate dehydrogenase in complex with isocitrate and Mn

Summary for 1ITW

• Entry DOI: 10.2210/pdb1itw/pdb
• Descriptor: Isocitrate dehydrogenase, MANGANESE (II) ION, ISOCITRIC ACID, ... (4 entities in total)
• Functional Keywords: greece key motif, oxidoreductase
• Biological source: Azotobacter vinelandii
• Cellular location: Cytoplasm: P16100
• Total number of polymer chains: 4
• Total formula weight: 323073.72

Authors

Yasutake, Y.,Watanabe, S.,Yao, M.,Takada, Y.,Fukunaga, N.,Tanaka, I. (deposition date: 2002-02-12, release date: 2002-12-11, Last modification date: 2023-12-27)

Primary citation

Yasutake, Y.,Watanabe, S.,Yao, M.,Takada, Y.,Fukunaga, N.,Tanaka, I.
Structure of the Monomeric Isocitrate Dehydrogenase: Evidence of a Protein Monomerization by a Domain Duplication
Structure, 10:1637-1648, 2002

PubMed Abstract: NADP(+)-dependent isocitrate dehydrogenase is a member of the beta-decarboxylating dehydrogenase family and catalyzes the oxidative decarboxylation reaction from 2R,3S-isocitrate to yield 2-oxoglutarate and CO(2) in the Krebs cycle. Although most prokaryotic NADP(+)-dependent isocitrate dehydrogenases (IDHs) are homodimeric enzymes, the monomeric IDH with a molecular weight of 80-100 kDa has been found in a few species of bacteria. The 1.95 A crystal structure of the monomeric IDH revealed that it consists of two distinct domains, and its folding topology is related to the dimeric IDH. The structure of the large domain repeats a motif observed in the dimeric IDH. Such a fusional structure by domain duplication enables a single polypeptide chain to form a structure at the catalytic site that is homologous to the dimeric IDH, the catalytic site of which is located at the interface of two identical subunits.

PubMed: 12467571
DOI: 10.1016/S0969-2126(02)00904-8

Experimental method

X-RAY DIFFRACTION (1.95 Å)