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| | <StructureSection load='5dst' size='340' side='right'caption='[[5dst]], [[Resolution|resolution]] 2.96Å' scene=''> | | <StructureSection load='5dst' size='340' side='right'caption='[[5dst]], [[Resolution|resolution]] 2.96Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dst]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DST FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dst]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DST FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.963Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRMT8, HRMT1L3, HRMT1L4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dst OCA], [http://pdbe.org/5dst PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dst RCSB], [http://www.ebi.ac.uk/pdbsum/5dst PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dst 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=5dst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dst OCA], [https://pdbe.org/5dst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dst RCSB], [https://www.ebi.ac.uk/pdbsum/5dst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dst ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ANM8_HUMAN ANM8_HUMAN]] Membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS.<ref>PMID:16051612</ref> <ref>PMID:17925405</ref> <ref>PMID:18320585</ref> | + | [https://www.uniprot.org/uniprot/ANM8_HUMAN ANM8_HUMAN] Membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS.<ref>PMID:16051612</ref> <ref>PMID:17925405</ref> <ref>PMID:18320585</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5dst" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5dst" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Shimizu, T]] | + | [[Category: Shimizu T]] |
| - | [[Category: Toma-Fukai, S]] | + | [[Category: Toma-Fukai S]] |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
ANM8_HUMAN Membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS.[1] [2] [3]
Publication Abstract from PubMed
Protein arginine methyltransferase 8 (PRMT8) is unique among PRMTs, as it is specifically expressed in brain and localized to the plasma membrane via N-terminal myristoylation. Here, we describe the crystal structure of human PRMT8 (hPRMT8) at 3.0A resolution. The crystal structure of hPRMT8 exhibited a novel helical assembly. Biochemical, biophysical and mutagenesis experiments demonstrated that hPRMT8 forms an octamer in solution. This octameric structure is necessary for proper localization to the plasma membrane and efficient methyltransferase activity. The helical assembly might be a relevant quaternary form for hPRMT1, which is the predominant PRMT in mammalian cells and most closely related to hPRMT8.
Novel helical assembly in arginine methyltransferase 8.,Toma-Fukai S, Kim JD, Park KE, Kuwabara N, Shimizu N, Krayukuhina E, Uchiyama S, Fukamizu A, Shimizu T J Mol Biol. 2016 Feb 11. pii: S0022-2836(16)00112-1. doi:, 10.1016/j.jmb.2016.02.007. PMID:26876602[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee J, Sayegh J, Daniel J, Clarke S, Bedford MT. PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. J Biol Chem. 2005 Sep 23;280(38):32890-6. Epub 2005 Jul 28. PMID:16051612 doi:http://dx.doi.org/M506944200
- ↑ Sayegh J, Webb K, Cheng D, Bedford MT, Clarke SG. Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain. J Biol Chem. 2007 Dec 14;282(50):36444-53. Epub 2007 Oct 9. PMID:17925405 doi:http://dx.doi.org/10.1074/jbc.M704650200
- ↑ Pahlich S, Zakaryan RP, Gehring H. Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state. Proteins. 2008 Sep;72(4):1125-37. doi: 10.1002/prot.22004. PMID:18320585 doi:http://dx.doi.org/10.1002/prot.22004
- ↑ Toma-Fukai S, Kim JD, Park KE, Kuwabara N, Shimizu N, Krayukuhina E, Uchiyama S, Fukamizu A, Shimizu T. Novel helical assembly in arginine methyltransferase 8. J Mol Biol. 2016 Feb 11. pii: S0022-2836(16)00112-1. doi:, 10.1016/j.jmb.2016.02.007. PMID:26876602 doi:http://dx.doi.org/10.1016/j.jmb.2016.02.007
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