4PFK

PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL

4PFK の概要

• エントリーDOI: 10.2210/pdb4pfk/pdb
• 分子名称: PHOSPHOFRUCTOKINASE, 6-O-phosphono-beta-D-fructofuranose, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: transferase(phosphotransferase)
• 由来する生物種: Geobacillus stearothermophilus
• 細胞内の位置: Cytoplasm: P00512
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35330.01

構造登録者

Evans, P.R.,Hudson, P.J. (登録日: 1988-01-25, 公開日: 1989-01-09, 最終更新日: 2024-02-28)

主引用文献

Evans, P.R.,Farrants, G.W.,Hudson, P.J.
Phosphofructokinase: structure and control.
Philos.Trans.R.Soc.London,Ser.B, 293:53-62, 1981

PubMed Abstract: Phosphofructokinase from Bacillus stearothermophilus shows cooperative kinetics with respect to the substrate fructose-6-phosphate (F6P), allosteric activation by ADP, and inhibition by phosphoenolpyruvate. The crystal structure of the active conformation of the enzyme has been solved to 2.4 A resolution, and three ligand-binding sites have been located. Two of these form the active site and bind the substrates F6P and ATP. The third site binds both allosteric activator and inhibitor. The complex of the enzyme with F6P and ADP has been partly refined at 2.4 A resolution, and a model of ATP has been built into the active site by using the refined model of ADP and a 6 A resolution map of bound 5'-adenylylimidodiphosphate (AMPPNP). The gamma-phosphate of ATP is close to the 1-hydroxyl of F6P, in a suitable position for in-line phosphoryl transfer. The binding of the phosphate of F6P involves two arginines from a neighbouring subunit in the tetramer, which suggests that a rearrangement of the subunits could explain the cooperativity of substrate binding. The activatory ADP is also bound by residues from two subunits.

PubMed: 6115424

実験手法

X-RAY DIFFRACTION (2.4 Å)