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1zkk

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(New page: 200px<br /> <applet load="1zkk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zkk, resolution 1.45&Aring;" /> '''Crystal structure o...)
Current revision (09:05, 14 February 2024) (edit) (undo)
 
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[[Image:1zkk.gif|left|200px]]<br />
 
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<applet load="1zkk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zkk, resolution 1.45&Aring;" />
 
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'''Crystal structure of hSET8 in ternary complex with H4 peptide (16-24) and AdoHcy'''<br />
 
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==Overview==
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==Crystal structure of hSET8 in ternary complex with H4 peptide (16-24) and AdoHcy==
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SET8 (also known as PR-SET7) is a histone H4-Lys-20-specific, methyltransferase that is implicated in cell-cycle-dependent, transcriptional silencing and mitotic regulation in metazoans. Herein we, report the crystal structure of human SET8 (hSET8) bound to a histone H4, peptide bearing Lys-20 and the product cofactor S-adenosylhomocysteine., Histone H4 intercalates in the substrate-binding cleft as an extended, parallel beta-strand. Residues preceding Lys-20 in H4 engage in an, extensive array of salt bridge, hydrogen bond, and van der Waals, interactions with hSET8, while the C-terminal residues bind through, predominantly hydrophobic interactions. Mutational analysis of both the, substrate-binding cleft and histone H4 reveals that interactions with, residues in the N and C termini of the H4 peptide are critical for, conferring substrate specificity. Finally, analysis of the product, specificity indicates that hSET8 is a monomethylase, consistent with its, role in the maintenance of Lys-20 monomethylation during cell division.
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<StructureSection load='1zkk' size='340' side='right'caption='[[1zkk]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zkk]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZKK FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zkk OCA], [https://pdbe.org/1zkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zkk RCSB], [https://www.ebi.ac.uk/pdbsum/1zkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zkk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KMT5A_HUMAN KMT5A_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. Plays a negative role in TGF-beta response regulation and a positive role in cell migration.<ref>PMID:12086618</ref> <ref>PMID:12121615</ref> <ref>PMID:15200950</ref> <ref>PMID:15933069</ref> <ref>PMID:15933070</ref> <ref>PMID:16517599</ref> <ref>PMID:17707234</ref> <ref>PMID:23478445</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zk/1zkk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zkk ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ZKK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SAH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZKK OCA].
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase., Couture JF, Collazo E, Brunzelle JS, Trievel RC, Genes Dev. 2005 Jun 15;19(12):1455-65. Epub 2005 Jun 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15933070 15933070]
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__TOC__
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[[Category: Histone-lysine N-methyltransferase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brunzelle, J.S.]]
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[[Category: Brunzelle JS]]
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[[Category: Collazo, E.]]
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[[Category: Collazo E]]
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[[Category: Couture, J.F.]]
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[[Category: Couture J-F]]
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[[Category: Trievel, R.C.]]
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[[Category: Trievel RC]]
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[[Category: SAH]]
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[[Category: beta-sheet]]
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[[Category: histone h4]]
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[[Category: pseudo-knot]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:35:53 2007''
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Current revision

Crystal structure of hSET8 in ternary complex with H4 peptide (16-24) and AdoHcy

PDB ID 1zkk

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