2IAE

Crystal structure of a protein phosphatase 2A (PP2A) holoenzyme.

2IAE の概要

• エントリーDOI: 10.2210/pdb2iae/pdb
• 関連するPDBエントリー: 1B3U
• 関連するBIRD辞書のPRD_ID: PRD_000212
• 分子名称: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform, Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform, Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, ... (5 entities in total)
• 機能のキーワード: protein phosphorylation, phosphatase, pp2a, b56, tumor suppressor, methylation, hydrolase, toxin, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Cytoplasm : Q76MZ3 P67775; Nucleus: Q13362
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 300705.13

構造登録者

Cho, U.S.,Xu, W. (登録日: 2006-09-07, 公開日: 2006-12-26, 最終更新日: 2023-11-15)

主引用文献

Cho, U.S.,Xu, W.
Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme.
Nature, 445:53-57, 2007

PubMed Abstract: Protein phosphatase 2A (PP2A) is a principal Ser/Thr phosphatase, the deregulation of which is associated with multiple human cancers, Alzheimer's disease and increased susceptibility to pathogen infections. How PP2A is structurally organized and functionally regulated remains unclear. Here we report the crystal structure of an AB'C heterotrimeric PP2A holoenzyme. The structure reveals that the HEAT repeats of the scaffold A subunit form a horseshoe-shaped fold, holding the catalytic C and regulatory B' subunits together on the same side. The regulatory B' subunit forms pseudo-HEAT repeats and interacts with the C subunit near the active site, thereby defining substrate specificity. The methylated carboxy-terminal tail of the C subunit interacts with a highly negatively charged region at the interface between A and B' subunits, suggesting that the C-terminal carboxyl methylation of the C subunit promotes B' subunit recruitment by neutralizing charge repulsion. Together, our structural results establish a crucial foundation for understanding PP2A assembly, substrate recruitment and regulation.

PubMed: 17086192
DOI: 10.1038/nature05351

実験手法

X-RAY DIFFRACTION (3.5 Å)