1RJD
Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity
Summary for 1RJD
| Entry DOI | 10.2210/pdb1rjd/pdb |
| Descriptor | carboxy methyl transferase for protein phosphatase 2A catalytic subunit, S-ADENOSYLMETHIONINE, BETA-MERCAPTOETHANOL, ... (5 entities in total) |
| Functional Keywords | sam dependent methyltransferase, transferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 3 |
| Total formula weight | 117462.49 |
| Authors | 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. (deposition date: 2003-11-19, release date: 2003-12-02, Last modification date: 2011-07-13) |
| Primary citation | 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 Cited by 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: 14660564DOI: 10.1074/jbc.M311484200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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