Crystallographic studies on the activity of glycogen phosphorylase b
- 1 August 1978
- journal article
- Published by Springer Nature in Nature
- Vol. 274 (5670), 433-437
- https://doi.org/10.1038/274433a0
Abstract
High resolution studies on the crystal structure of glycogen phosphorylase b have identified the catalytic site to which the substrate glucose-1-phosphate binds strongly with some local conformational changes. The site is situated 8 A (phosphate-to-phosphate distance) from pyridoxal phosphate, an essential cofactor of all glycogen phosphorylases. The catalytic site is 33 A from the site in the N-terminal portion of the molecule to which adenine nucleotides bind. In contrast to phosphorylase a (the active form of the enzyme which is phosphorylated at Ser 14), the positions of the first 19 residues of phosphorylase b are not well defined.Keywords
This publication has 33 references indexed in Scilit:
- Crystallographic analysis at low resolution of metabolite binding sites on phosphorylase bJournal of Molecular Biology, 1978
- Crystal structure of bovine trypsinogen at 1·8 Å resolutionJournal of Molecular Biology, 1977
- The crystal structure of phosphorylase b at 6 Å resolutionJournal of Molecular Biology, 1974
- Chemical and biological evolution of a nucleotide-binding proteinNature, 1974
- A tetragonal crystal form of phosphorylase bJournal of Molecular Biology, 1972
- The mode of binding of pyridoxal 5′-phosphate in glycogen phosphorylaseBiochemical and Biophysical Research Communications, 1970
- Distinct amp binding sites in glycogen phosphorylase b as revealed by calorimetric studiesBiochemical and Biophysical Research Communications, 1970
- Studies on the helical conformational of amylose and possible interconversionsBiopolymers, 1969
- The Crystal and Molecular Structure of the Cyclohexaamylose-Potassium Acetate Complex1Journal of the American Chemical Society, 1965
- THE REACTION OF SODIUM BOROHYDRIDE WITH MUSCLE PHOSPHORYLASE1Journal of the American Chemical Society, 1958