4ij8

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{{STRUCTURE_4ij8| PDB=4ij8 | SCENE= }}
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==Crystal structure of the complex of SETD8 with SAM==
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===Crystal structure of the complex of SETD8 with SAM===
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<StructureSection load='4ij8' size='340' side='right' caption='[[4ij8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[4ij8]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Miscellaneous_nucleic_acid Miscellaneous nucleic acid]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IJ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IJ8 FirstGlance]. <br>
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</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=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETD8, KMT5A, PRSET7, SET07, SET8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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=4ij8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ij8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ij8 RCSB], [http://www.ebi.ac.uk/pdbsum/4ij8 PDBsum]</span></td></tr>
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</table>
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== Function ==
[[http://www.uniprot.org/uniprot/SETD8_HUMAN SETD8_HUMAN]] Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes.<ref>PMID:12086618</ref> <ref>PMID:12121615</ref> <ref>PMID:15200950</ref> <ref>PMID:16517599</ref> <ref>PMID:17707234</ref> <ref>PMID:15933069</ref> <ref>PMID:15933070</ref>
[[http://www.uniprot.org/uniprot/SETD8_HUMAN SETD8_HUMAN]] Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes.<ref>PMID:12086618</ref> <ref>PMID:12121615</ref> <ref>PMID:15200950</ref> <ref>PMID:16517599</ref> <ref>PMID:17707234</ref> <ref>PMID:15933069</ref> <ref>PMID:15933070</ref>
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==About this Structure==
 
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[[4ij8]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Miscellaneous_nucleic_acid Miscellaneous nucleic acid]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IJ8 OCA].
 
==See Also==
==See Also==
*[[Histone methyltransferase|Histone methyltransferase]]
*[[Histone methyltransferase|Histone methyltransferase]]
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== References ==
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==Reference==
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<references/>
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<references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Miscellaneous nucleic acid]]
[[Category: Miscellaneous nucleic acid]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Arrowsmith, C H]]
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[[Category: Bakkouri, M El.]]
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[[Category: Bakkouri, M El]]
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[[Category: Bountra, C.]]
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[[Category: Bountra, C]]
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[[Category: Brown, P J.]]
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[[Category: Brown, P J]]
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[[Category: Edwards, A M.]]
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[[Category: Edwards, A M]]
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[[Category: Li, Y.]]
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[[Category: Li, Y]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Structural genomic]]
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[[Category: Shapira, M.]]
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[[Category: Shapira, M]]
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[[Category: Tempel, W.]]
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[[Category: Tempel, W]]
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[[Category: Yu, W.]]
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[[Category: Yu, W]]
[[Category: N-lysine methyltransferase]]
[[Category: N-lysine methyltransferase]]
[[Category: Sgc]]
[[Category: Sgc]]
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[[Category: Structural genomics consortium]]
 
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 11:18, 25 December 2014

Crystal structure of the complex of SETD8 with SAM

4ij8, resolution 2.00Å

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