3ua3: Difference between revisions
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==Crystal Structure of Protein Arginine Methyltransferase PRMT5 in complex with SAH== | ==Crystal Structure of Protein Arginine Methyltransferase PRMT5 in complex with SAH== | ||
<StructureSection load='3ua3' size='340' side='right' caption='[[3ua3]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='3ua3' size='340' side='right'caption='[[3ua3]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ua3]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ua3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UA3 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='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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ua4|3ua4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ua4|3ua4]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prmt-5 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prmt-5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-arginine_N-methyltransferase Histone-arginine N-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.125 2.1.1.125] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ua3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ua3 OCA], [https://pdbe.org/3ua3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ua3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ua3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ua3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/ANM5_CAEEL ANM5_CAEEL]] Symmetrically methylates arginine residues in proteins such as small nuclear ribonucleoproteins or histone H2A/H4. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Caeel]] | [[Category: Caeel]] | ||
[[Category: Histone-arginine N-methyltransferase]] | [[Category: Histone-arginine N-methyltransferase]] | ||
[[Category: Large Structures]] | |||
[[Category: Bao, S]] | [[Category: Bao, S]] | ||
[[Category: Gong, W]] | [[Category: Gong, W]] | ||
Revision as of 09:04, 13 July 2022
Crystal Structure of Protein Arginine Methyltransferase PRMT5 in complex with SAHCrystal Structure of Protein Arginine Methyltransferase PRMT5 in complex with SAH
Structural highlights
Function[ANM5_CAEEL] Symmetrically methylates arginine residues in proteins such as small nuclear ribonucleoproteins or histone H2A/H4. Publication Abstract from PubMedSymmetric and asymmetric dimethylation of arginine are isomeric protein posttranslational modifications with distinct biological effects, evidenced by the methylation of arginine 3 of histone H4 (H4R3): symmetric dimethylation of H4R3 leads to repression of gene expression, while asymmetric dimethylation of H4R3 is associated with gene activation. The enzymes catalyzing these modifications share identifiable sequence similarities, but the relationship between their catalytic mechanisms is unknown. Here we analyzed the structure of a prototypic symmetric arginine dimethylase, PRMT5, and discovered that a conserved phenylalanine in the active site is critical for specifying symmetric addition of methyl groups. Changing it to a methionine significantly elevates the overall methylase activity, but also converts PRMT5 to an enzyme that catalyzes both symmetric and asymmetric dimethylation of arginine. Our results demonstrate a common catalytic mechanism intrinsic to both symmetric and asymmetric arginine dimethylases, and show that steric constrains in the active sites play an essential role in determining the product specificity of arginine methylases. This discovery also implies a potentially regulatable outcome of arginine dimethylation that may provide versatile control of eukaryotic gene expression. Structural insights into protein arginine symmetric dimethylation by PRMT5.,Sun L, Wang M, Lv Z, Yang N, Liu Y, Bao S, Gong W, Xu RM Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20538-43. Epub 2011 Dec 5. PMID:22143770[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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