2HV6

Crystal structure of the phosphotyrosyl phosphatase activator

2HV6 の概要

• エントリーDOI: 10.2210/pdb2hv6/pdb
• 分子名称: Protein phosphatase 2A, regulatory subunit B, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: phosphotyrosyl phosphatase activator, phosphatase, pp2a, phosphatase specificity, unknown function
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q15257
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73662.54

構造登録者

Chao, Y.,Jeffrey, P.D.,Shi, Y. (登録日: 2006-07-27, 公開日: 2006-08-22, 最終更新日: 2023-08-30)

主引用文献

Chao, Y.,Xing, Y.,Chen, Y.,Xu, Y.,Lin, Z.,Li, Z.,Jeffrey, P.D.,Stock, J.B.,Shi, Y.
Structure and mechanism of the phosphotyrosyl phosphatase activator.
Mol.Cell, 23:535-546, 2006

PubMed Abstract: Phosphotyrosyl phosphatase activator (PTPA), also known as PP2A phosphatase activator, is a conserved protein from yeast to human. Here we report the 1.9 A crystal structure of human PTPA, which reveals a previously unreported fold consisting of three subdomains: core, lid, and linker. Structural analysis uncovers a highly conserved surface patch, which borders the three subdomains, and an associated deep pocket located between the core and the linker subdomains. The conserved surface patch and the deep pocket are responsible for binding to PP2A and ATP, respectively. PTPA and PP2A A-C dimer together constitute a composite ATPase. PTPA binding to PP2A results in a dramatic alteration of substrate specificity, with enhanced phosphotyrosine phosphatase activity and decreased phosphoserine phosphatase activity. This function of PTPA strictly depends on the composite ATPase activity. These observations reveal significant insights into the function and mechanism of PTPA and have important ramifications for understanding PP2A function.

PubMed: 16916641
DOI: 10.1016/j.molcel.2006.07.027

実験手法

X-RAY DIFFRACTION (1.9 Å)