1FJM

Protein serine/threonine phosphatase-1 (alpha isoform, type 1) complexed with microcystin-LR toxin

1FJM の概要

• エントリーDOI: 10.2210/pdb1fjm/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000212
• 分子名称: PROTEIN SERINE/THREONINE PHOSPHATASE-1 (ALPHA ISOFORM, TYPE 1), microcystin LR, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, toxin, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Oryctolagus cuniculus (rabbit); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 77520.51

構造登録者

Goldberg, J.,Nairn, A.C.,Kuriyan, J. (登録日: 1995-12-17, 公開日: 1996-06-20, 最終更新日: 2023-11-15)

主引用文献

Goldberg, J.,Huang, H.B.,Kwon, Y.G.,Greengard, P.,Nairn, A.C.,Kuriyan, J.
Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1.
Nature, 376:745-753, 1995

PubMed Abstract: The crystal structure of mammalian protein phosphatase-1, complexed with the toxin microcystin and determined at 2.1 A resolution, reveals that it is a metalloenzyme unrelated in architecture to the tyrosine phosphatases. Two metal ions are positioned by a central beta-alpha-beta-alpha-beta scaffold at the active site, from which emanate three surface grooves that are potential binding sites for substrates and inhibitors. The carboxy terminus is positioned at the end of one of the grooves such that regulatory sequences following the domain might modulate function. The fold of the catalytic domain is expected to be closely preserved in protein phosphatases 2A and 2B (calcineurin).

PubMed: 7651533
DOI: 10.1038/376745a0

実験手法

X-RAY DIFFRACTION (2.1 Å)