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4bup
From Proteopedia
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| - | + | ==A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases== | |
| - | + | <StructureSection load='4bup' size='340' side='right' caption='[[4bup]], [[Resolution|resolution]] 2.17Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4bup]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BUP FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4au7|4au7]]</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=4bup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bup OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bup RCSB], [http://www.ebi.ac.uk/pdbsum/4bup PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/SV421_MOUSE SV421_MOUSE]] 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).<ref>PMID:15145825</ref> | [[http://www.uniprot.org/uniprot/SV421_MOUSE SV421_MOUSE]] 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).<ref>PMID:15145825</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The delivery of site-specific post-translational modifications to histones generates an epigenetic regulatory network that directs fundamental DNA-mediated processes and governs key stages in development. Methylation of histone H4 lysine-20 has been implicated in DNA repair, transcriptional silencing, genomic stability and regulation of replication. We present the structure of the histone H4K20 methyltransferase Suv4-20h2 in complex with its histone H4 peptide substrate and S-adenosyl methionine cofactor. Analysis of the structure reveals that the Suv4-20h2 active site diverges from the canonical SET domain configuration and generates a high degree of both substrate and product specificity. Together with supporting biochemical data comparing Suv4-20h1 and Suv4-20h2, we demonstrate that the Suv4-20 family enzymes take a previously mono-methylated H4K20 substrate and generate an exclusively di-methylated product. We therefore predict that other enzymes are responsible for the tri-methylation of histone H4K20 that marks silenced heterochromatin. | ||
| + | |||
| + | A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases.,Southall SM, Cronin NB, Wilson JR Nucleic Acids Res. 2013 Sep 18. PMID:24049080<ref>PMID:24049080</ref> | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[Histone methyltransferase|Histone methyltransferase]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
| - | [[Category: Cronin, N B | + | [[Category: Cronin, N B]] |
| - | [[Category: Southall, S M | + | [[Category: Southall, S M]] |
| - | [[Category: Wilson, J R | + | [[Category: Wilson, J R]] |
[[Category: Epigenetic]] | [[Category: Epigenetic]] | ||
[[Category: Histone]] | [[Category: Histone]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 13:51, 25 December 2014
A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases
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