1MKP

CRYSTAL STRUCTURE OF PYST1 (MKP3)

1MKP の概要

• エントリーDOI: 10.2210/pdb1mkp/pdb
• 分子名称: PYST1, CHLORIDE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q16828
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16428.28

構造登録者

Stewart, A.E.,Dowd, S.,Keyse, S.,Mcdonald, N.Q. (登録日: 1998-07-11, 公開日: 1999-07-22, 最終更新日: 2024-02-14)

主引用文献

Stewart, A.E.,Dowd, S.,Keyse, S.M.,McDonald, N.Q.
Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation.
Nat.Struct.Biol., 6:174-181, 1999

PubMed Abstract: The crystal structure of the catalytic domain from the MAPK phosphatase Pyst1 (Pyst1-CD) has been determined at 2.35 A. The structure adopts a protein tyrosine phosphatase (PTPase) fold with a shallow active site that displays a distorted geometry in the absence of its substrate with some similarity to the dual-specificity phosphatase cdc25. Functional characterization of Pyst1-CD indicates it is sufficient to dephosphorylate activated ERK2 in vitro. Kinetic analysis of Pyst1 and Pyst1-CD using the substrate p-nitrophenyl phosphate (pNPP) reveals that both molecules undergo catalytic activation in the presence of recombinant inactive ERK2, switching from a low- to high-activity form. Mutation of Asp 262, located 5.5 A distal to the active site, demonstrates it is essential for catalysis in the high-activity ERK2-dependent conformation of Pyst1 but not for the low-activity ERK2-independent form, suggesting that ERK2 induces closure of the Asp 262 loop over the active site, thereby enhancing Pyst1 catalytic efficiency.

PubMed: 10048930
DOI: 10.1038/5861

実験手法

X-RAY DIFFRACTION (2.35 Å)