1S95

Structure of serine/threonine protein phosphatase 5

1S95 の概要

• エントリーDOI: 10.2210/pdb1s95/pdb
• 分子名称: Serine/threonine protein phosphatase 5, MANGANESE (II) ION, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: protein phosphatase, pppase, pp5, phosphate anion, metal ion, metallophosphoesterase, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : P53041
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76420.08

構造登録者

Swingle, M.R.,Honkanen, R.E.,Ciszak, E.M. (登録日: 2004-02-03, 公開日: 2004-08-24, 最終更新日: 2023-08-23)

主引用文献

Swingle, M.R.,Honkanen, R.E.,Ciszak, E.M.
Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5.
J.Biol.Chem., 279:33992-33999, 2004

PubMed Abstract: Serine/threonine protein phosphatase-5 (PP5) affects many signaling networks that regulate cell growth and cellular responses to stress. Here we report the crystal structure of the PP5 catalytic domain (PP5c) at a resolution of 1.6 A. From this structure we propose a mechanism for PP5-mediated hydrolysis of phosphoprotein substrates, which requires the precise positioning of two metal ions within a conserved Asp271-M1:M2-W1-His427-His304-Asp274 catalytic motif (where M1 and M2 are metals and W1 is a water molecule). The structure of PP5c provides a structural basis for explaining the exceptional catalytic proficiency of protein phosphatases, which are among the most powerful known catalysts. Resolution of the entire C terminus revealed a novel subdomain, and the structure of the PP5c should also aid development of type-specific inhibitors.

PubMed: 15155720
DOI: 10.1074/jbc.M402855200

実験手法

X-RAY DIFFRACTION (1.6 Å)