1rjf
|
Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity
OverviewOverview
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.
About this StructureAbout this Structure
1RJF is a Single protein structure of sequence from Saccharomyces cerevisiae with BME and GOL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structure of protein phosphatase methyltransferase 1 (PPM1), a leucine carboxyl methyltransferase involved in the regulation of protein phosphatase 2A activity., Leulliot N, Quevillon-Cheruel S, Sorel I, de La Sierra-Gallay IL, Collinet B, Graille M, Blondeau K, Bettache N, Poupon A, Janin J, van Tilbeurgh H, J Biol Chem. 2004 Feb 27;279(9):8351-8. Epub 2003 Dec 4. PMID:14660564
Page seeded by OCA on Wed Nov 21 01:38:43 2007