1G0H

CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE-FRUCTOSE 1,6 BISPHOSPHATASE

1G0H の概要

• エントリーDOI: 10.2210/pdb1g0h/pdb
• 関連するPDBエントリー: 1DK4 1G0I
• 分子名称: INOSITOL MONOPHOSPHATASE, CALCIUM ION, D-MYO-INOSITOL-1-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: homodimer, complexed with ca2+ and i-1-p, hydrolase
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57900.23

構造登録者

Johnson, K.A.,Chen, L.,Yang, H.,Roberts, M.F.,Stec, B. (登録日: 2000-10-06, 公開日: 2001-03-14, 最終更新日: 2023-08-09)

主引用文献

Johnson, K.A.,Chen, L.,Yang, H.,Roberts, M.F.,Stec, B.
Crystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities.
Biochemistry, 40:618-630, 2001

PubMed Abstract: Inositol monophosphatase (EC 3.1.3.25) in hyperthermophilic archaea is thought to play a role in the biosynthesis of di-myo-inositol-1,1'-phosphate (DIP), an osmolyte unique to hyperthermophiles. The Methanococcus jannaschii MJ109 gene product, the sequence of which is substantially homologous to that of human inositol monophosphatase, exhibits inositol monophosphatase activity but with substrate specificity that is broader than those of bacterial and eukaryotic inositol monophosphatases (it can also act as a fructose bisphosphatase). To understand its substrate specificity as well as the poor inhibition by Li(+) (a potent inhibitor of the mammalian enzyme), we have crystallized the enzyme and determined its three-dimensional structure. The overall fold, as expected, is similar to that of the mammalian enzyme, but the details suggest a closer relationship to fructose 1,6-bisphosphatases. Three complexes of the MJ0109 protein with substrate and/or product and inhibitory as well as activating metal ions suggest that the phosphatase mechanism is a three-metal ion assisted catalysis which is in variance with that proposed previously for the human inositol monophosphatase.

PubMed: 11170378
DOI: 10.1021/bi0016422

実験手法

X-RAY DIFFRACTION (2.3 Å)