The binding of β-glycerophosphate to glycogen phosphorylase b in the crystal

N. G. Oikonomakos, K. R. Acharya, A. E. Melpidou, D. I. Stuart, L. N. Johnson

Research output: Contribution to journalArticle

Abstract

The binding of β-glycerophosphate (glycerol-2-P) to glycogen phosphorylase b in the crystal has been studied by X-ray diffraction at 3 Å 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.

Original languageEnglish
Pages (from-to)62-68
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume270
Issue number1
DOIs
Publication statusPublished - 1 Jan 1989

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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