Crystallographic studies on the activity of glycogen phosphorylase b
Authors:
- I. T. WeberIWI. T. Weber
- L. N. JohnsonLJL. N. Johnson
- K. S. WilsonKWK. S. Wilson
- D. G. R. YeatesDYD. G. R. Yeates
- D. L. WildDWD. L. Wild
- J. A. JenkinsJJJ. A. Jenkins
- 1 August 1978
- journal article
- Published by Springer Nature in Nature
- Vol. 274 (5670) , 433-437
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
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