2NYL

Crystal structure of Protein Phosphatase 2A (PP2A) holoenzyme with the catalytic subunit carboxyl terminus truncated

2NYL の概要

• エントリーDOI: 10.2210/pdb2nyl/pdb
• 関連するPDBエントリー: 2IE3 2IE4 2NPP 2NYM
• 関連するBIRD辞書のPRD_ID: PRD_000212
• 分子名称: Protein phosphatase 2, regulatory subunit A (PR 65), 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: heat repeat, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q13362; Cytoplasm : P67775
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 293245.11

構造登録者

Xing, Y.,Xu, Y.,Chen, Y.,Chao, Y.,Lin, Z.,Shi, Y. (登録日: 2006-11-20, 公開日: 2006-12-12, 最終更新日: 2023-11-15)

主引用文献

Xu, Y.,Xing, Y.,Chen, Y.,Chao, Y.,Lin, Z.,Fan, E.,Yu, J.W.,Strack, S.,Jeffrey, P.D.,Shi, Y.
Structure of the Protein Phosphatase 2A Holoenzyme.
Cell(Cambridge,Mass.), 127:1239-1251, 2006

PubMed Abstract: Protein Phosphatase 2A (PP2A) plays an essential role in many aspects of cellular physiology. The PP2A holoenzyme consists of a heterodimeric core enzyme, which comprises a scaffolding subunit and a catalytic subunit, and a variable regulatory subunit. Here we report the crystal structure of the heterotrimeric PP2A holoenzyme involving the regulatory subunit B'/B56/PR61. Surprisingly, the B'/PR61 subunit has a HEAT-like (huntingtin-elongation-A subunit-TOR-like) repeat structure, similar to that of the scaffolding subunit. The regulatory B'/B56/PR61 subunit simultaneously interacts with the catalytic subunit as well as the conserved ridge of the scaffolding subunit. The carboxyterminus of the catalytic subunit recognizes a surface groove at the interface between the B'/B56/PR61 subunit and the scaffolding subunit. Compared to the scaffolding subunit in the PP2A core enzyme, formation of the holoenzyme forces the scaffolding subunit to undergo pronounced conformational rearrangements. This structure reveals significant ramifications for understanding the function and regulation of PP2A.

PubMed: 17174897
DOI: 10.1016/j.cell.2006.11.033

実験手法

X-RAY DIFFRACTION (3.8 Å)