7w9v
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7w9v]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=7W9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W9V FirstGlance]. <br> | <table><tr><td colspan='2'>[[7w9v]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=7W9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W9V 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=7w9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w9v OCA], [https://pdbe.org/7w9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w9v RCSB], [https://www.ebi.ac.uk/pdbsum/7w9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w9v 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]] 3.95Å</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=7w9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w9v OCA], [https://pdbe.org/7w9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w9v RCSB], [https://www.ebi.ac.uk/pdbsum/7w9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w9v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/H31_HUMAN H31_HUMAN] | |
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | p300 is a human acetyltransferase that associates with chromatin and mediates vital cellular processes. We now report the cryo-electron microscopy structures of the p300 catalytic core in complex with the nucleosome core particle (NCP). In the most resolved structure, the HAT domain and bromodomain of p300 contact nucleosomal DNA at superhelical locations 2 and 3, and the catalytic site of the HAT domain are positioned near the N-terminal tail of histone H4. Mutations of the p300-DNA interfacial residues of p300 substantially decrease binding to NCP. Three additional classes of p300-NCP complexes show different modes of the p300-NCP complex formation. Our data provide structural details critical to our understanding of the mechanism by which p300 acetylates multiple sites on the nucleosome. | ||
+ | |||
+ | Structural basis for binding diversity of acetyltransferase p300 to the nucleosome.,Hatazawa S, Liu J, Takizawa Y, Zandian M, Negishi L, Kutateladze TG, Kurumizaka H iScience. 2022 Jun 9;25(7):104563. doi: 10.1016/j.isci.2022.104563. eCollection , 2022 Jul 15. PMID:35754730<ref>PMID:35754730</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7w9v" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Histone 3D structures|Histone 3D structures]] | ||
+ | *[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
Cryo-EM structure of nucleosome in complex with p300 acetyltransferase catalytic core (complex I)
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