1rjf: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
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...
 
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1rjf.jpg|left|200px]]<br /><applet load="1rjf" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rjf, resolution 2.25&Aring;" />
'''Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity'''<br />


==Overview==
==Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity==
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.
<StructureSection load='1rjf' size='340' side='right'caption='[[1rjf]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1rjf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJF FirstGlance]. <br>
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RJF OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rjf OCA], [https://pdbe.org/1rjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rjf RCSB], [https://www.ebi.ac.uk/pdbsum/1rjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rjf ProSAT]</span></td></tr>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14660564 14660564]
</table>
== Function ==
[https://www.uniprot.org/uniprot/LCMT1_YEAST LCMT1_YEAST] Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. Acts on the two major protein phosphatase 2A catalytic subunits, PPH21 and PPH22.<ref>PMID:11060018</ref> <ref>PMID:11697862</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/1rjf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rjf ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Bettache N]]
[[Category: Bettache, N.]]
[[Category: Blondeau K]]
[[Category: Blondeau, K.]]
[[Category: Collinet B]]
[[Category: Collinet, B.]]
[[Category: Graille M]]
[[Category: Graille, M.]]
[[Category: Janin J]]
[[Category: Janin, J.]]
[[Category: Leulliot N]]
[[Category: Leulliot, N.]]
[[Category: Poupon A]]
[[Category: Poupon, A.]]
[[Category: Quevillon-Cheruel S]]
[[Category: Quevillon-Cheruel, S.]]
[[Category: Sorel I]]
[[Category: Sierra-Gallay, I.L.de.La.]]
[[Category: De La Sierra-Gallay IL]]
[[Category: Sorel, I.]]
[[Category: Van Tilbeurgh H]]
[[Category: Tilbeurgh, H.van.]]
[[Category: BME]]
[[Category: GOL]]
[[Category: sam dependent methyltransferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:38:43 2007''

Latest revision as of 11:23, 14 February 2024

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

Structural highlights

1rjf is a 3 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LCMT1_YEAST Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. Acts on the two major protein phosphatase 2A catalytic subunits, PPH21 and PPH22.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Wu J, Tolstykh T, Lee J, Boyd K, Stock JB, Broach JR. Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo. EMBO J. 2000 Nov 1;19(21):5672-81. PMID:11060018 doi:http://dx.doi.org/10.1093/emboj/19.21.5672
  2. ↑ Kalhor HR, Luk K, Ramos A, Zobel-Thropp P, Clarke S. Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity responsible for modification of the major forms of protein phosphatase 2A in yeast. Arch Biochem Biophys. 2001 Nov 15;395(2):239-45. PMID:11697862 doi:http://dx.doi.org/10.1006/abbi.2001.2558

1rjf, resolution 2.25Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1rjf&oldid=4054410"