1CNQ

FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH FRUCTOSE-6-PHOSPHATE AND ZINC IONS

「1BFL」から置き換えられました

1CNQ の概要

• エントリーDOI: 10.2210/pdb1cnq/pdb
• 分子名称: FRUCTOSE-1,6-BISPHOSPHATASE, 6-O-phosphono-beta-D-fructofuranose, ZINC ION, ... (5 entities in total)
• 機能のキーワード: bisphosphatase, 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: 37502.68

構造登録者

Choe, J.,Poland, B.W.,Fromm, H.,Honzatko, R. (登録日: 1999-05-21, 公開日: 1999-05-28, 最終更新日: 2024-05-22)

主引用文献

Choe, J.Y.,Poland, B.W.,Fromm, H.J.,Honzatko, R.B.
Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase.
Biochemistry, 37:11441-11450, 1998

PubMed Abstract: A disordered loop (loop 52-72, residues 52-72) in crystal structures of fructose-1,6-bisphosphatase (FBPase) has been implicated in regulatory and catalytic phenomena by studies in directed mutation. A crystal structure of FBPase in a complex with three zinc cations and the products fructose 6-phosphate (F6P) and phosphate (Pi) reveals loop 52-72 for the first time in a well-defined conformation with strong electron density. Loop 52-57 interacts primarily with the active site of its own subunit. Asp68 of the loop hydrogen bonds with Arg276 and a zinc cation located at the putative potassium activation site. Leu56 and Tyr57 of the loop pack against hydrophobic residues from two separate subunits of FBPase. A mechanism of allosteric regulation of catalysis is presented, in which AMP, by binding to its allosteric pocket, displaces loop 52-72 from the active site. Furthermore, the current structure suggests that both the alpha- and beta-anomers of F6P can be substrates in the reverse reaction catalyzed by FBPase. Mechanisms of catalysis are proposed for the reverse reaction in which Asp121 serves as a catalytic base for the alpha-anomer and Glu280 serves as a catalytic base for the beta-anomer.

PubMed: 9708979
DOI: 10.1021/bi981112u

実験手法

X-RAY DIFFRACTION (2.27 Å)