1rjg: Difference between revisions

Revision as of 06:30, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1rjg.png

Template:STRUCTURE 1rjg

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

Template:ABSTRACT PUBMED 14660564

About this StructureAbout this Structure

1RJG is a Single protein structure of sequence from Saccharomyces cerevisiae. 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

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OCA

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-'''Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity'''
+===Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity===
-==Overview==
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-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.
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 [[Category: Tilbeurgh, H van.]]
 [[Category: Sam dependent methyltransferase]]
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