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The binding of beta-glycerophosphate (glycerol-2-P) to glycogen phosphorylase b in the crystal has been studied by X-ray diffraction at 3 A resolution. Glycerol-2-P binds to the allosteric effector site in a position close to that of AMP, glucose-6-P, UDP-Glc, and phosphate. In this position, glycerol-2-P is stabilized through interactions of its phosphate moiety with the guanidinium groups of Arg 309 and Arg 310 which undergo conformational changes, and the hydroxyl group of Tyr 75, while the same residues and solvent are involved in van der Waals interactions with the remaining part of the molecule. Kinetic experiments indicate that glycerol-2-P partially competes with both the activator (AMP) and the inhibitor (glucose 6-phosphate) of phosphorylase b. A comparison of the positions of glycerol-2-P, AMP, glucose 6-phosphate, UDP-Glc, and Pi at the allosteric site is presented.

Type

Journal article

Journal

Arch Biochem Biophys

Publication Date

04/1989

Volume

270

Pages

62 - 68

Keywords

Adenosine Monophosphate, Animals, Binding Sites, Binding, Competitive, Glucose-6-Phosphate, Glucosephosphates, Glycerophosphates, Kinetics, Molecular Conformation, Muscles, Phosphorylase b, Phosphorylases, Rabbits, Statistics as Topic, X-Ray Diffraction