3PFK

PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL

Summary for 3PFK

• Entry DOI: 10.2210/pdb3pfk/pdb
• Descriptor: PHOSPHOFRUCTOKINASE, PHOSPHATE ION (3 entities in total)
• Functional Keywords: transferase(phosphotransferase)
• Biological source: Geobacillus stearothermophilus
• Cellular location: Cytoplasm: P00512
• Total number of polymer chains: 1
• Total formula weight: 34356.81

Authors

Evans, P.R.,Hudson, P.J. (deposition date: 1988-01-25, release date: 1989-01-09, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)