1RJG

Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity

1RJG の概要

• エントリーDOI: 10.2210/pdb1rjg/pdb
• 関連するPDBエントリー: 1RJD 1RJE 1RJF
• 分子名称: carboxy methyl transferase for protein phosphatase 2A catalytic subunit, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: sam dependent methyltransferase, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38951.85

構造登録者

Leulliot, N.,Quevillon-Cheruel, S.,Sorel, I.,Li de La Sierra-Gallay, I.,Collinet, B.,Graille, M.,Blondeau, K.,Bettache, N.,Poupon, A.,Janin, J.,van Tilbeurgh, H. (登録日: 2003-11-19, 公開日: 2003-12-02, 最終更新日: 2023-08-23)

主引用文献

Leulliot, N.,Quevillon-Cheruel, S.,Sorel, I.,Li de La Sierra-Gallay, I.,Collinet, B.,Graille, M.,Blondeau, K.,Bettache, N.,Poupon, A.,Janin, J.,van Tilbeurgh, H.
Structure of protein phosphatase methyltransferase 1 (PPM1), a leucine carboxyl methyltransferase involved in the regulation of protein phosphatase 2A activity
J.Biol.Chem., 279:8351-8358, 2004

PubMed Abstract: The important role of the serine/threonine protein phosphatase 2A (PP2A) in various cellular processes requires a precise and dynamic regulation of PP2A activity, localization, and substrate specificity. The regulation of the function of PP2A involves the reversible methylation of the COOH group of the C-terminal leucine of the catalytic subunit, which, in turn, controls the enzyme's heteromultimeric composition and confers different protein recognition and substrate specificity. We have determined the structure of PPM1, the yeast methyltransferase responsible for methylation of PP2A. The structure of PPM1 reveals a common S-adenosyl-l-methionine-dependent methyltransferase fold, with several insertions conferring the specific function and substrate recognition. The complexes with the S-adenosyl-l-methionine methyl donor and the S-adenosyl-l-homocysteine product and inhibitor unambiguously revealed the co-substrate binding site and provided a convincing hypothesis for the PP2A C-terminal peptide binding site. The structure of PPM1 in a second crystal form provides clues to the dynamic nature of the PPM1/PP2A interaction.

PubMed: 14660564
DOI: 10.1074/jbc.M311484200

実験手法

X-RAY DIFFRACTION (2.61 Å)