6nj9

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==Active state Dot1L bound to the H2B-Ubiquitinated nucleosome, 2-to-1 complex==
==Active state Dot1L bound to the H2B-Ubiquitinated nucleosome, 2-to-1 complex==
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<StructureSection load='6nj9' size='340' side='right' caption='[[6nj9]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
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<SX load='6nj9' size='340' side='right' viewer='molstar' caption='[[6nj9]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6nj9]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NJ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NJ9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6nj9]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NJ9 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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.96&#8491;</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=NLE:NORLEUCINE'>NLE</scene></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=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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<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>
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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=6nj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nj9 OCA], [https://pdbe.org/6nj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nj9 RCSB], [https://www.ebi.ac.uk/pdbsum/6nj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nj9 ProSAT]</span></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=6nj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nj9 OCA], [http://pdbe.org/6nj9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nj9 RCSB], [http://www.ebi.ac.uk/pdbsum/6nj9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nj9 ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[[http://www.uniprot.org/uniprot/H32_XENLA H32_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H2B11_XENLA H2B11_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H2A1_XENLA H2A1_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H4_XENLA H4_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/DOT1L_HUMAN DOT1L_HUMAN]] Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA.
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== Publication Abstract from PubMed ==
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Methylation of histone H3 K79 by Dot1L is a hallmark of actively transcribed genes that depends on monoubiquitination of H2B K120 (H2B-Ub) and is an example of histone modification cross-talk that is conserved from yeast to humans. We report here cryo-EM structures of Dot1L bound to ubiquitinated nucleosome that show how H2B-Ub stimulates Dot1L activity and reveal a role for the histone H4 tail in positioning Dot1L. We find that contacts mediated by Dot1L and the H4 tail induce a conformational change in the globular core of histone H3 that reorients K79 from an inaccessible position, thus enabling this side chain to insert into the active site in a position primed for catalysis. Our study provides a comprehensive mechanism of cross-talk between histone ubiquitination and methylation and reveals structural plasticity in histones that makes it possible for histone-modifying enzymes to access residues within the nucleosome core.
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Mechanism of Cross-talk between H2B Ubiquitination and H3 Methylation by Dot1L.,Worden EJ, Hoffmann NA, Hicks CW, Wolberger C Cell. 2019 Feb 8. pii: S0092-8674(19)30151-5. doi: 10.1016/j.cell.2019.02.002. PMID:30765112<ref>PMID:30765112</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6nj9" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Histone 3D structures|Histone 3D structures]]
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Histone-lysine N-methyltransferase]]
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[[Category: Homo sapiens]]
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[[Category: Hoffmann, N A]]
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[[Category: Large Structures]]
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[[Category: Wolberger, C]]
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[[Category: Synthetic construct]]
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[[Category: Worden, E J]]
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[[Category: Xenopus laevis]]
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[[Category: Methyltransferase]]
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[[Category: Hoffmann NA]]
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[[Category: Nucleosome]]
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[[Category: Wolberger C]]
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[[Category: Structural protein-transferase-dna complex]]
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[[Category: Worden EJ]]
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[[Category: Ubiquitin]]
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Current revision

Active state Dot1L bound to the H2B-Ubiquitinated nucleosome, 2-to-1 complex

6nj9, resolution 2.96Å

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