This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1rjf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1rjf.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1rjf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rjf| PDB=1rjf | SCENE= }}
{{STRUCTURE_1rjf| PDB=1rjf | SCENE= }}
-
'''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==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14660564}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14660564 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14660564}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Tilbeurgh, H van.]]
[[Category: Tilbeurgh, H van.]]
[[Category: Sam dependent methyltransferase]]
[[Category: Sam dependent methyltransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:34:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:14:02 2008''

Revision as of 11:14, 29 July 2008

Image:1rjf.png

Template:STRUCTURE 1rjf

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

Template:ABSTRACT PUBMED 14660564

About this Structure

1RJF is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

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 Tue Jul 29 14:14:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rjf"
Personal tools