9GPB

THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE

9GPB の概要

• エントリーDOI: 10.2210/pdb9gpb/pdb
• 分子名称: GLYCOGEN PHOSPHORYLASE B, SULFATE ION, PYRIDOXAL-5'-PHOSPHATE (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: 391306.14

構造登録者

Barford, D.,Johnson, L.N. (登録日: 1990-12-17, 公開日: 1992-10-15, 最終更新日: 2017-11-29)

主引用文献

Barford, D.,Johnson, L.N.
The allosteric transition of glycogen phosphorylase.
Nature, 340:609-616, 1989

PubMed Abstract: The crystal structure of R-state glycogen phosphorylase b has been determined at 2.9 A resolution. A comparison of T-state and R-state structures of the enzyme explains its cooperative behaviour on ligand binding and the allosteric regulation of its activity. Communication between catalytic sites of the dimer is provided by a change in packing geometry of two helices linking each site with the subunit interface. Activation by AMP or by phosphorylation results in a quaternary conformational change that switches these two helices into the R-state conformation.

PubMed: 2770867
DOI: 10.1038/340609a0

実験手法

X-RAY DIFFRACTION (2.9 Å)