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{{STRUCTURE_3s8p|  PDB=3s8p  |  SCENE=  }}
==Crystal Structure of the SET Domain of Human Histone-Lysine N-Methyltransferase SUV420H1 In Complex With S-Adenosyl-L-Methionine==
===Crystal Structure of the SET Domain of Human Histone-Lysine N-Methyltransferase SUV420H1 In Complex With S-Adenosyl-L-Methionine===
<StructureSection load='3s8p' size='340' side='right' caption='[[3s8p]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
{{ABSTRACT_PUBMED_24396869}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3s8p]] is a 2 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=3S8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S8P FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CGI-85, KMT5B, SUV420H1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></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=3s8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s8p RCSB], [http://www.ebi.ac.uk/pdbsum/3s8p PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SUV420H1 and SUV420H2 are two highly homologous enzymes that methylate lysine 20 of histone H4 (H4K20), a mark that has been implicated in transcriptional regulation. In this study, we present the high-resolution crystal structures of human SUV420H1 and SUV420H2 in complex with SAM, and report their substrate specificity. Both methyltransferases have a unique N-terminal domain and Zn-binding post-SET domain, and prefer the monomethylated histone H4K20 as a substrate in vitro. No histone H4K20 trimethylation activity was detected by our radioactivity-based assay for either enzyme, consistent with the presence of a conserved serine residue that forms a hydrogen bond with the target lysine side-chain and limits the methylation level.


==Function==
Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2.,Wu H, Siarheyeva A, Zeng H, Lam R, Dong A, Wu XH, Li Y, Schapira M, Vedadi M, Min J FEBS Lett. 2013 Nov 29;587(23):3859-68. PMID:24396869<ref>PMID:24396869</ref>
[[http://www.uniprot.org/uniprot/SV421_HUMAN SV421_HUMAN]] Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity).  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3s8p]] is a 2 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=3S8P OCA].
</div>


==See Also==
==See Also==
*[[Histone methyltransferase|Histone methyltransferase]]
*[[Histone methyltransferase|Histone methyltransferase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:024396869</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Human]]
[[Category: Human]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith, C H]]
[[Category: Bountra, C.]]
[[Category: Bountra, C]]
[[Category: Edwards, A M.]]
[[Category: Edwards, A M]]
[[Category: Lam, R.]]
[[Category: Lam, R]]
[[Category: Loppnau, P.]]
[[Category: Loppnau, P]]
[[Category: Min, J.]]
[[Category: Min, J]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Structural genomic]]
[[Category: Weigelt, J.]]
[[Category: Weigelt, J]]
[[Category: Wu, H.]]
[[Category: Wu, H]]
[[Category: Zeng, H.]]
[[Category: Zeng, H]]
[[Category: Chromosome]]
[[Category: Chromosome]]
[[Category: Histone lysine]]
[[Category: Histone lysine]]
Line 34: Line 44:
[[Category: Set domain]]
[[Category: Set domain]]
[[Category: Sgc]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Transferase]]
[[Category: Transferase]]
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