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3s8p
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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=== | ||
| - | {{ABSTRACT_PUBMED_24396869}} | ||
| - | == | + | ==Crystal Structure of the SET Domain of Human Histone-Lysine N-Methyltransferase SUV420H1 In Complex With S-Adenosyl-L-Methionine== |
| - | [[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). | + | <StructureSection load='3s8p' size='340' side='right'caption='[[3s8p]], [[Resolution|resolution]] 1.85Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3s8p]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3S8P FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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 ([https://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'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3s8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s8p OCA], [https://pdbe.org/3s8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s8p RCSB], [https://www.ebi.ac.uk/pdbsum/3s8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s8p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://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). | ||
| + | <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> | |
| + | <div class="pdbe-citations 3s8p" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| - | [[Category: Arrowsmith, C H | + | [[Category: Large Structures]] |
| - | [[Category: Bountra, C | + | [[Category: Arrowsmith, C H]] |
| - | [[Category: Edwards, A M | + | [[Category: Bountra, C]] |
| - | [[Category: Lam, R | + | [[Category: Edwards, A M]] |
| - | [[Category: Loppnau, P | + | [[Category: Lam, R]] |
| - | [[Category: Min, J | + | [[Category: Loppnau, P]] |
| - | [[Category: | + | [[Category: Min, J]] |
| - | [[Category: Weigelt, J | + | [[Category: Structural genomic]] |
| - | [[Category: Wu, H | + | [[Category: Weigelt, J]] |
| - | [[Category: Zeng, H | + | [[Category: Wu, H]] |
| + | [[Category: Zeng, H]] | ||
[[Category: Chromosome]] | [[Category: Chromosome]] | ||
[[Category: Histone lysine]] | [[Category: Histone lysine]] | ||
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[[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]] | ||
Current revision
Crystal Structure of the SET Domain of Human Histone-Lysine N-Methyltransferase SUV420H1 In Complex With S-Adenosyl-L-Methionine
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Categories: Histone-lysine N-methyltransferase | Human | Large Structures | Arrowsmith, C H | Bountra, C | Edwards, A M | Lam, R | Loppnau, P | Min, J | Structural genomic | Weigelt, J | Wu, H | Zeng, H | Chromosome | Histone lysine | Histone methyltransferase | Methylation | Nucleus | Sam | Set domain | Sgc | Transcription regulation | Transferase
