1RM0

Crystal Structure of Myo-Inositol 1-Phosphate Synthase From Saccharomyces cerevisiae In Complex With NAD+ and 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate

1RM0 の概要

• エントリーDOI: 10.2210/pdb1rm0/pdb
• 分子名称: myo-inositol-phosphate synthase, MANGANESE (II) ION, (3,4,5,7-TETRAHYDROXY-HEPT-1-ENYL)-PHOSPHONIC ACID, ... (5 entities in total)
• 機能のキーワード: myo-inositol 1-phosphate synthase, isomerase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 121043.52

構造登録者

Jin, X.,Foley, K.M.,Geiger, J.H. (登録日: 2003-11-26, 公開日: 2004-05-25, 最終更新日: 2024-02-14)

主引用文献

Jin, X.,Foley, K.M.,Geiger, J.H.
The structure of the 1L-myo-inositol-1-phosphate synthase-NAD+-2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex demands a revision of the enzyme mechanism.
J.Biol.Chem., 279:13889-13895, 2004

PubMed Abstract: 1l-myo-inositol 1-phosphate (MIP) synthase catalyzes the conversion of d-glucose 6-phosphate to 1l-myo-inositol 1-phosphate, the first and rate-limiting step in the biosynthesis of all inositol-containing compounds. It involves an oxidation, enolization, intramolecular aldol cyclization, and reduction. Here we present the structure of MIP synthase in complex with NAD(+) and a high-affinity inhibitor, 2-deoxy-d-glucitol 6-(E)-vinylhomophosphonate. This structure reveals interactions between the enzyme active site residues and the inhibitor that are significantly different from that proposed for 2-deoxy-d-glucitol 6-phosphate in the previously published structure of MIP synthase-NAD(+)-2-deoxy-d-glucitol 6-phosphate. There are several other conformational changes in NAD(+) and the enzyme active site as well. Based on the new structural data, we propose a new and completely different mechanism for MIP synthase.

PubMed: 14684747
DOI: 10.1074/jbc.M308986200

実験手法

X-RAY DIFFRACTION (2.05 Å)