1ITW

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

1ITW の概要

• エントリーDOI: 10.2210/pdb1itw/pdb
• 分子名称: Isocitrate dehydrogenase, MANGANESE (II) ION, ISOCITRIC ACID, ... (4 entities in total)
• 機能のキーワード: greece key motif, oxidoreductase
• 由来する生物種: Azotobacter vinelandii
• 細胞内の位置: Cytoplasm: P16100
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 323073.72

構造登録者

Yasutake, Y.,Watanabe, S.,Yao, M.,Takada, Y.,Fukunaga, N.,Tanaka, I. (登録日: 2002-02-12, 公開日: 2002-12-11, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.95 Å)