Structural basis of the allosteric behaviour of phosphofructokinase.
Comparison between the crystal structures of low- and high-affinity forms of phosphofructokinase shows a close coupling between the change of quaternary structure and local changes triggered by binding of the allosteric effectors. These concerted changes link all the substrate and effector sites in the tetramer, and explain the change of affinity for the cooperative substrate.
Schirmer
T
T
MRC Laboratory of Molecular Biology, Cambridge, UK.
Evans
P R
PR
D000494:Allosteric Regulation; D000495:Allosteric Site; D000595:Amino Acid Sequence; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D011487:Protein Conformation
D046911:Macromolecular Substances; D010732:Phosphofructokinase-1