1PYG

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

1PYG の概要

• エントリーDOI: 10.2210/pdb1pyg/pdb
• 分子名称: GLYCOGEN PHOSPHORYLASE B, ADENOSINE MONOPHOSPHATE, PYRIDOXAL-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: glycogen phosphorylase
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 391862.18

構造登録者

Sprang, S. (登録日: 1992-07-07, 公開日: 1994-01-31, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.87 Å)