1PYG

STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE

Summary for 1PYG

• Entry DOI: 10.2210/pdb1pyg/pdb
• Descriptor: GLYCOGEN PHOSPHORYLASE B, ADENOSINE MONOPHOSPHATE, PYRIDOXAL-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: glycogen phosphorylase
• Biological source: Oryctolagus cuniculus (rabbit)
• Total number of polymer chains: 4
• Total formula weight: 391862.18

Authors

Sprang, S. (deposition date: 1992-07-07, release date: 1994-01-31, Last modification date: 2024-10-30)

Primary citation

Sprang, S.R.,Withers, S.G.,Goldsmith, E.J.,Fletterick, R.J.,Madsen, N.B.
Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate.
Science, 254:1367-1371, 1991

PubMed Abstract: The three-dimensional structure of the activated state of glycogen phosphorylase (GP) as induced by adenosine monophosphate (AMP) has been determined from crystals of pyridoxalpyrophosphoryl-GP. The same quaternary changes relative to the inactive conformation as those induced by phosphorylation are induced by AMP, although the two regulatory signals function through different local structural mechanisms. Moreover, previous descriptions of the phosphorylase active state have been extended by demonstrating that, on activation, the amino- and carboxyl-terminal domains of GP rotate apart by 5 degrees, thereby increasing access of substrates to the catalytic site. The structure also reveals previously unobserved interactions with the nucleotide that accounts for the specificity of the nucleotide binding site for AMP in preference to inosine monophosphate.

PubMed: 1962195

Experimental method

X-RAY DIFFRACTION (2.87 Å)