6wk2: Difference between revisions
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<StructureSection load='6wk2' size='340' side='right'caption='[[6wk2]], [[Resolution|resolution]] 1.76Å' scene=''> | <StructureSection load='6wk2' size='340' side='right'caption='[[6wk2]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6wk2]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6wk2]] is a 4 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=6WK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WK2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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=6wk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wk2 OCA], [https://pdbe.org/6wk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wk2 RCSB], [https://www.ebi.ac.uk/pdbsum/6wk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wk2 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SETD3_HUMAN SETD3_HUMAN] Histone methyltransferase that methylates 'Lys-36' of histone H3 (H3K36me). H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation (By similarity). | ||
<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 6wk2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6wk2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cheng X]] | |||
[[Category: Cheng | [[Category: Dai S]] | ||
[[Category: Dai | [[Category: Horton JR]] | ||
[[Category: Horton | |||
Latest revision as of 17:28, 18 October 2023
SETD3 mutant (N255V) in Complex with an Actin Peptide with His73 Replaced with MethionineSETD3 mutant (N255V) in Complex with an Actin Peptide with His73 Replaced with Methionine
Structural highlights
FunctionSETD3_HUMAN Histone methyltransferase that methylates 'Lys-36' of histone H3 (H3K36me). H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation (By similarity). Publication Abstract from PubMedMost characterized protein methylation events encompass arginine and lysine N-methylation, and only a few cases of protein methionine thiomethylation have been reported. Newly discovered oncohistone mutations include lysine-to-methionine substitutions at positions 27 and 36 of histone H3.3. In these instances, the methionine substitution localizes to the active-site pocket of the corresponding histone lysine methyltransferase, thereby inhibiting the respective transmethylation activity. SET domain-containing 3 (SETD3) is a protein (i.e. actin) histidine methyltransferase. Here, we generated an actin variant in which the histidine target of SETD3 was substituted with methionine. As for previously characterized histone SET domain proteins, the methionine substitution substantially (76-fold) increased binding affinity for SETD3 and inhibited SETD3 activity on histidine. Unexpectedly, SETD3 was active on the substituted methionine, generating S-methylmethionine in the context of actin peptide. The ternary structure of SETD3 in complex with the methionine-containing actin peptide at 1.9 A resolution revealed that the hydrophobic thioether side chain is packed by the aromatic rings of Tyr312 and Trp273 as well as the hydrocarbon side chain of Ile310. Our results suggest that placing methionine properly in the active site-within close proximity to and in line with the incoming methyl group of SAM-would allow some SET domain proteins to selectively methylate methionine in proteins. Characterization of SETD3 methyltransferase mediated protein methionine methylation.,Dai S, Holt MV, Horton JR, Woodcock CB, Patel A, Zhang X, Young NL, Wilkinson AW, Cheng X J Biol Chem. 2020 Jun 5. pii: RA120.014072. doi: 10.1074/jbc.RA120.014072. PMID:32503840[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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