1EYI

FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH MAGNESIUM, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (R-STATE)

1EYI の概要

• エントリーDOI: 10.2210/pdb1eyi/pdb
• 関連するPDBエントリー: 1CNQ 1EYJ 1EYK
• 分子名称: FRUCTOSE-1,6-BISPHOSPHATASE, 6-O-phosphono-beta-D-fructofuranose, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: bisphosphatase, allosteric enzymes, gluconeogenesis, hydrolase
• 由来する生物種: Sus scrofa (pig)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37189.90

構造登録者

Choe, J.,Honzatko, R.B. (登録日: 2000-05-06, 公開日: 2000-08-09, 最終更新日: 2023-08-09)

主引用文献

Choe, J.Y.,Fromm, H.J.,Honzatko, R.B.
Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes.
Biochemistry, 39:8565-8574, 2000

PubMed Abstract: Crystal structures of metal-product complexes of fructose 1, 6-bisphosphatase (FBPase) reveal competition between AMP and divalent cations. In the presence of AMP, the Zn(2+)-product and Mg(2+)-product complexes have a divalent cation present only at one of three metal binding sites (site 1). The enzyme is in the T-state conformation with a disordered loop of residues 52-72 (loop 52-72). In the absence of AMP, the enzyme crystallizes in the R-state conformation, with loop 52-72 associated with the active site. In structures without AMP, three metal-binding sites are occupied by Zn(2+) and two of three metal sites (sites 1 and 2) by Mg(2+). Evidently, the association of AMP with FBPase disorders loop 52-72, the consequence of which is the release of cations from two of three metal binding sites. In the Mg(2+) complexes (but not the Zn(2+) complexes), the 1-OH group of fructose 6-phosphate (F6P) coordinates to the metal at site 1 and is oriented for a nucleophilic attack on the bound phosphate molecule. A mechanism is presented for the forward reaction, in which Asp74 and Glu98 together generate a hydroxide anion coordinated to the Mg(2+) at site 2, which then displaces F6P. Development of negative charge on the 1-oxygen of F6P is stabilized by its coordination to the Mg(2+) at site 1.

PubMed: 10913263
DOI: 10.1021/bi000574g

実験手法

X-RAY DIFFRACTION (2.32 Å)