1JKI

myo-Inositol-1-phosphate Synthase Complexed with an Inhibitor, 2-deoxy-glucitol-6-phosphate

1JKI の概要

• エントリーDOI: 10.2210/pdb1jki/pdb
• 関連するPDBエントリー: 1JKF
• 分子名称: myo-inositol-1-phosphate synthase, AMMONIUM ION, 2-DEOXY-GLUCITOL-6-PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: rossmann fold, inhibitor-bound structure, isomerase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P11986
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 121274.79

構造登録者

Stein, A.J.,Geiger, J.H. (登録日: 2001-07-12, 公開日: 2002-04-10, 最終更新日: 2023-08-16)

主引用文献

Stein, A.J.,Geiger, J.H.
The crystal structure and mechanism of 1-L-myo-inositol- 1-phosphate synthase
J.Biol.Chem., 277:9484-9491, 2002

PubMed Abstract: 1-l-myo-Inositol-1-phosphate synthase catalyzes the conversion of d-glucose 6-phosphate to 1-l-myo-inositol-1-phosphate (MIP), the first and rate-limiting step in the biosynthesis of all inositol-containing compounds. It involves an oxidation, intramolecular aldol cyclization, and reduction. We have determined the first crystal structure of MIP synthase. We present structures of both the NAD-bound enzyme and the enzyme bound to an inhibitor, 2-deoxy-glucitol-6-phosphate. While 58 amino acids are disordered in the unbound form of the enzyme in the vicinity of the active site, the inhibitor nucleates the folding of this domain in a striking example of induced fit, serving to completely encapsulate it within the enzyme. Three helices and a long beta-strand are formed in this process. We postulate a mechanism for the conversion based on the structure of the inhibitor-bound complex.

PubMed: 11779862
DOI: 10.1074/jbc.M109371200
主引用文献が同じPDBエントリー

実験手法

X-RAY DIFFRACTION (2.2 Å)