1rje
From Proteopedia
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| - | [[Image:1rje.png|left|200px]] | ||
| - | + | ==Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity== | |
| - | + | <StructureSection load='1rje' size='340' side='right'caption='[[1rje]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1rje]] 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=1RJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJE FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | == | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rje OCA], [https://pdbe.org/1rje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rje RCSB], [https://www.ebi.ac.uk/pdbsum/1rje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rje ProSAT]</span></td></tr> |
| - | [[1rje]] is a 3 chain structure with sequence from [ | + | </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/1rje_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=1rje ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Bettache | + | [[Category: Bettache N]] |
| - | [[Category: Blondeau | + | [[Category: Blondeau K]] |
| - | [[Category: Collinet | + | [[Category: Collinet B]] |
| - | [[Category: Graille | + | [[Category: Graille M]] |
| - | [[Category: Janin | + | [[Category: Janin J]] |
| - | [[Category: Leulliot | + | [[Category: Leulliot N]] |
| - | [[Category: Poupon | + | [[Category: Poupon A]] |
| - | [[Category: Quevillon-Cheruel | + | [[Category: Quevillon-Cheruel S]] |
| - | [[Category: | + | [[Category: Sorel I]] |
| - | [[Category: | + | [[Category: De La Sierra-Gallay IL]] |
| - | [[Category: Tilbeurgh | + | [[Category: Van Tilbeurgh H]] |
| - | + | ||
| - | + | ||
Current revision
Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity
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