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3rq4
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of suppressor of variegation 4-20 homolog 2== | |
| - | + | <StructureSection load='3rq4' size='340' side='right' caption='[[3rq4]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3rq4]] is a 1 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=3RQ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RQ4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SUV420H2, KMT5C, PP7130 ([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=3rq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rq4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rq4 RCSB], [http://www.ebi.ac.uk/pdbsum/3rq4 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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
==See Also== | ==See Also== | ||
*[[Histone methyltransferase|Histone methyltransferase]] | *[[Histone methyltransferase|Histone methyltransferase]] | ||
| - | + | == References == | |
| - | == | + | <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: Dong, A | + | [[Category: Dong, A]] |
| - | [[Category: Edwards, A M | + | [[Category: Edwards, A M]] |
| - | [[Category: Loppnau, P | + | [[Category: Loppnau, P]] |
| - | [[Category: Min, J | + | [[Category: Min, J]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Tempel, W | + | [[Category: Tempel, W]] |
| - | [[Category: Weigelt, J | + | [[Category: Weigelt, J]] |
| - | [[Category: Wu, H | + | [[Category: Wu, H]] |
| - | [[Category: Zeng, H | + | [[Category: Zeng, H]] |
[[Category: Sgc]] | [[Category: Sgc]] | ||
| - | [[Category: Structural genomic]] | ||
| - | [[Category: Structural genomics consortium]] | ||
[[Category: Suppressor]] | [[Category: Suppressor]] | ||
[[Category: Suv420h2]] | [[Category: Suv420h2]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Variegation 4-20 homolog 2]] | [[Category: Variegation 4-20 homolog 2]] | ||
Revision as of 16:37, 21 December 2014
Crystal structure of suppressor of variegation 4-20 homolog 2
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