7k6q
From Proteopedia
(Difference between revisions)
(New page: ==== <StructureSection load='7k6q' size='340' side='right'caption='7k6q' scene=''> == Structural highlights == <table><tr><td colspan='2'>Full crystallographic information is availabl...) |
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| - | ==== | + | ==Active state Dot1 bound to the H4K16ac nucleosome== |
| - | <StructureSection load='7k6q' size='340' side='right'caption='[[7k6q]]' scene=''> | + | <StructureSection load='7k6q' size='340' side='right'caption='[[7k6q]], [[Resolution|resolution]] 3.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7k6q]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae], [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=7K6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K6Q FirstGlance]. <br> |
| - | </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=7k6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k6q OCA], [https://pdbe.org/7k6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k6q RCSB], [https://www.ebi.ac.uk/pdbsum/7k6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k6q ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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=7k6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k6q OCA], [https://pdbe.org/7k6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k6q RCSB], [https://www.ebi.ac.uk/pdbsum/7k6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k6q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Dot1 (disruptor of telomeric silencing-1), the histone H3 lysine 79 (H3K79) methyltransferase, is conserved throughout evolution, and its deregulation is found in human leukemias. Here, we provide evidence that acetylation of histone H4 allosterically stimulates yeast Dot1 in a manner distinct from but coordinating with histone H2B ubiquitination (H2BUb). We further demonstrate that this stimulatory effect is specific to acetylation of lysine 16 (H4K16ac), a modification central to chromatin structure. We provide a mechanism of this histone cross-talk and show that H4K16ac and H2BUb play crucial roles in H3K79 di- and trimethylation in vitro and in vivo. These data reveal mechanisms that control H3K79 methylation and demonstrate how H4K16ac, H3K79me, and H2BUb function together to regulate gene transcription and gene silencing to ensure optimal maintenance and propagation of an epigenetic state. | ||
| + | |||
| + | Regulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation.,Valencia-Sanchez MI, De Ioannes P, Wang M, Truong DM, Lee R, Armache JP, Boeke JD, Armache KJ Science. 2021 Jan 22;371(6527):eabc6663. doi: 10.1126/science.abc6663. PMID:33479126<ref>PMID:33479126</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7k6q" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Histone 3D structures|Histone 3D structures]] | ||
| + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | ||
| + | *[[3D structures of ubiquitin|3D structures of ubiquitin]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae]] |
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Xenopus laevis]] | ||
| + | [[Category: Armache J-P]] | ||
| + | [[Category: Armache K-J]] | ||
| + | [[Category: Boeke JD]] | ||
| + | [[Category: De Ioannes PE]] | ||
| + | [[Category: Lee R]] | ||
| + | [[Category: Miao W]] | ||
| + | [[Category: Truong DM]] | ||
| + | [[Category: Valencia-Sanchez MI]] | ||
Current revision
Active state Dot1 bound to the H4K16ac nucleosome
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