4g56

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==Crystal Structure of full length PRMT5/MEP50 complexes from Xenopus laevis==
==Crystal Structure of full length PRMT5/MEP50 complexes from Xenopus laevis==
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<StructureSection load='4g56' size='340' side='right' caption='[[4g56]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
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<StructureSection load='4g56' size='340' side='right'caption='[[4g56]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4g56]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G56 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G56 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4g56]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G56 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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hsl7, PRMT5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]), MEP50, MGC81050, wdr77 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4g56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g56 OCA], [https://pdbe.org/4g56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g56 RCSB], [https://www.ebi.ac.uk/pdbsum/4g56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g56 ProSAT]</span></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=4g56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g56 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g56 RCSB], [http://www.ebi.ac.uk/pdbsum/4g56 PDBsum]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ANM5_XENLA ANM5_XENLA] Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins; such methylation being required for the assembly and biogenesis of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation (By similarity). Methylates the arginine in the motif G-R-G-X-G in its substrates histone H2A, H2AFX and H4, producing both monomethylated and symmetrically dimethylated 'Arg-3'. Methylates nucleoplasmin at 'Arg-192', producing both monomethylated and symmetrically dimethylated 'Arg-192'. Involved in the DNA replication checkpoint. Promotes entry into mitosis by promoting the proteasomal degradation of wee2-a.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4g56" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Almo, S C]]
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[[Category: Almo SC]]
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[[Category: Bonanno, J]]
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[[Category: Bonanno J]]
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[[Category: Ho, M]]
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[[Category: Ho M]]
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[[Category: Structural genomic]]
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[[Category: Shechter D]]
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[[Category: Shechter, D]]
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[[Category: Wilczek C]]
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[[Category: Wilczek, C]]
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[[Category: Histone methylation]]
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[[Category: Protein arginine methyltransferase]]
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[[Category: Protein complex]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of full length PRMT5/MEP50 complexes from Xenopus laevis

PDB ID 4g56

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