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| | <StructureSection load='2ob2' size='340' side='right'caption='[[2ob2]], [[Resolution|resolution]] 1.92Å' scene=''> | | <StructureSection load='2ob2' size='340' side='right'caption='[[2ob2]], [[Resolution|resolution]] 1.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ob2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OB2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ob2]] 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=2OB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OB2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ob1|2ob1]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPM1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2ob2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ob2 OCA], [https://pdbe.org/2ob2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ob2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ob2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ob2 ProSAT]</span></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=2ob2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ob2 OCA], [https://pdbe.org/2ob2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ob2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ob2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ob2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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>
| + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Groves, M R]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Kreplin, X]] | + | [[Category: Groves MR]] |
| - | [[Category: Mueller, I B]] | + | [[Category: Kreplin X]] |
| - | [[Category: Mueller-Dieckmann, J]] | + | [[Category: Mueller IB]] |
| - | [[Category: Ppm1 without 1]]
| + | [[Category: Mueller-Dieckmann J]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
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.
Publication Abstract from PubMed
A technique is described whereby the addition of low concentrations (millimolar to micromolar) of the fluorescent dye 1,8-ANS to the protein solution prior to crystallization results in crystallization experiments in which protein crystals are strongly contrasted above background artifacts when exposed to low-intensity UV radiation. As 1,8-ANS does not covalently modify the protein sample, no further handling or purification steps are necessary. The system has been tested on a wide variety of protein samples and it has been shown that the addition of 1,8-ANS has no discernible effect on the crystallization frequencies or crystallization conditions of these proteins. As 1,8-ANS interacts with a wide variety of proteins, this is proposed to be a general solution for the automated classification of protein crystallization images and the detection of protein crystals. The results also demonstrate the expected discrimination between salt and protein crystals, as well as allowing the straightforward identification of small crystals that grow in precipitate or under a protein skin.
A method for the general identification of protein crystals in crystallization experiments using a noncovalent fluorescent dye.,Groves MR, Muller IB, Kreplin X, Muller-Dieckmann J Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):526-35. Epub 2007, Mar 16. PMID:17372358[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
- ↑ 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
- ↑ Groves MR, Muller IB, Kreplin X, Muller-Dieckmann J. A method for the general identification of protein crystals in crystallization experiments using a noncovalent fluorescent dye. Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):526-35. Epub 2007, Mar 16. PMID:17372358 doi:10.1107/S0907444906056137
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