5dst

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'''Unreleased structure'''
 
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The entry 5dst is ON HOLD until Paper Publication
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==Crystal structure of human PRMT8 in complex with SAH==
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<StructureSection load='5dst' size='340' side='right' caption='[[5dst]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5dst]] is a 15 chain structure. 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>
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</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>
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<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]</span></td></tr>
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</table>
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== Function ==
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[[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Toma-Fukai, S., Shimizu, T.
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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<ref>PMID:26876602</ref>
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Description: Crystal structure of human PRMT8 in complex with SAH
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Toma-Fukai, S]]
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<div class="pdbe-citations 5dst" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Shimizu, T]]
[[Category: Shimizu, T]]
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[[Category: Toma-Fukai, S]]
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[[Category: Methyltransferase]]
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[[Category: Transferase]]

Revision as of 18:09, 26 February 2016

Crystal structure of human PRMT8 in complex with SAH

5dst, resolution 2.96Å

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