1rjf: Difference between revisions
New page: left|200px<br /><applet load="1rjf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rjf, resolution 2.25Å" /> '''Structure of PPM1, a... |
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[[Image:1rjf.jpg|left|200px]]<br /><applet load="1rjf" size=" | [[Image:1rjf.jpg|left|200px]]<br /><applet load="1rjf" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1rjf, resolution 2.25Å" /> | caption="1rjf, resolution 2.25Å" /> | ||
'''Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity'''<br /> | '''Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity'''<br /> | ||
==Overview== | ==Overview== | ||
The important role of the serine/threonine protein phosphatase 2A (PP2A) | 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 Structure== | ==About this Structure== | ||
1RJF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with BME and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1RJF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=BME:'>BME</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJF OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Poupon, A.]] | [[Category: Poupon, A.]] | ||
[[Category: Quevillon-Cheruel, S.]] | [[Category: Quevillon-Cheruel, S.]] | ||
[[Category: Sierra-Gallay, I | [[Category: Sierra-Gallay, I L.de La.]] | ||
[[Category: Sorel, I.]] | [[Category: Sorel, I.]] | ||
[[Category: Tilbeurgh, H | [[Category: Tilbeurgh, H van.]] | ||
[[Category: BME]] | [[Category: BME]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: sam dependent methyltransferase]] | [[Category: sam dependent methyltransferase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:32 2008'' | ||
Revision as of 15:51, 21 February 2008
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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 and 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
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