1J1W

Crystal Structure Of The Monomeric Isocitrate Dehydrogenase In Complex With NADP+

1J1W の概要

• エントリーDOI: 10.2210/pdb1j1w/pdb
• 関連するPDBエントリー: 1ITW
• 分子名称: Isocitrate Dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: greek 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: 325004.15

構造登録者

Yasutake, Y.,Watanabe, S.,Yao, M.,Takada, Y.,Fukunaga, N.,Tanaka, I. (登録日: 2002-12-19, 公開日: 2003-09-23, 最終更新日: 2023-10-25)

主引用文献

Yasutake, Y.,Watanabe, S.,Yao, M.,Takada, Y.,Fukunaga, N.,Tanaka, I.
Crystal Structure of the Monomeric Isocitrate Dehydrogenase in the Presence of NADP+
J.Biol.Chem., 278:36897-36904, 2003

PubMed Abstract: NADP+-dependent monomeric isocitrate dehydrogenase (IDH) from the nitrogen-fixing bacterium Azotobacter vinelandii (AvIDH) is one of members of the beta-decarboxylating dehydrogenase family and catalyzes the dehydration and decarboxylation of isocitrate to yield 2-oxoglutrate and CO2 in the Krebs cycle. We solved the crystal structure of the AvIDH in complex with cofactor NADP+ (AvIDH-NADP+ complex). The final refined model shows the closed form that has never been detected in any previously solved structures of beta-decarboxylating dehydrogenases. The structure also reveals all of the residues that interact with NADP+. The structure-based sequence alignment reveals that these residues were not conserved in any other dimeric NADP+-dependent IDHs. Therefore the NADP+ specificity of the monomeric and dimeric IDHs was independently acquired through the evolutional process. The AvIDH was known to show an exceptionally high turnover rate. The structure of the AvIDH-NADP+ complex indicates that one loop, which is not present in the Escherichia coli IDHs, reliably stabilizes the conformation of the nicotinamide mononucleotide of the bound NADP+ by forming a few hydrogen bonds, and such interactions are considered to be important for the monomeric enzyme to initiate the hydride transfer reaction immediately. Finally, the structure of the AvIDH is compared with that of other dimeric NADP-IDHs. Several structural features demonstrate that the monomeric IDHs are structurally more related to the eukaryotic dimeric IDHs than to the bacterial dimeric IDHs.

PubMed: 12855708
DOI: 10.1074/jbc.M304091200

実験手法

X-RAY DIFFRACTION (3.2 Å)