6e86

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<StructureSection load='6e86' size='340' side='right' caption='[[6e86]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='6e86' size='340' side='right' caption='[[6e86]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6e86]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E86 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6e86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E86 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6e83|6e83]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6e83|6e83]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZZZ3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<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=6e86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e86 OCA], [http://pdbe.org/6e86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e86 RCSB], [http://www.ebi.ac.uk/pdbsum/6e86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e86 ProSAT]</span></td></tr>
<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=6e86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e86 OCA], [http://pdbe.org/6e86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e86 RCSB], [http://www.ebi.ac.uk/pdbsum/6e86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e86 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ZZZ3_HUMAN ZZZ3_HUMAN]] Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4.<ref>PMID:19103755</ref>
[[http://www.uniprot.org/uniprot/ZZZ3_HUMAN ZZZ3_HUMAN]] Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4.<ref>PMID:19103755</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Recognition of histones by epigenetic readers is a fundamental mechanism for the regulation of chromatin and transcription. Most reader modules target specific post-translational modifications on histones. Here, we report the identification of a reader of histone H3, the ZZ-type zinc finger (ZZ) domain of ZZZ3, a subunit of the Ada-two-A-containing (ATAC) histone acetyltransferase complex. The solution NMR structure of the ZZ in complex with the H3 peptide reveals a unique binding mechanism involving caging of the N-terminal Alanine 1 of histone H3 in an acidic cavity of the ZZ domain, indicating a specific recognition of H3 versus other histones. Depletion of ZZZ3 or disruption of the ZZ-H3 interaction dampens ATAC-dependent promoter histone H3K9 acetylation and target gene expression. Overall, our study identifies the ZZ domain of ZZZ3 as a histone H3 reader that is required for the ATAC complex-mediated maintenance of histone acetylation and gene activation.
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The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation.,Mi W, Zhang Y, Lyu J, Wang X, Tong Q, Peng D, Xue Y, Tencer AH, Wen H, Li W, Kutateladze TG, Shi X Nat Commun. 2018 Sep 14;9(1):3759. doi: 10.1038/s41467-018-06247-5. PMID:30217978<ref>PMID:30217978</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 6e86" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
[[Category: Kutateladze, T G]]
[[Category: Kutateladze, T G]]
[[Category: Zhang, Y]]
[[Category: Zhang, Y]]

Revision as of 08:48, 3 October 2018

Solution structure of ZZZ3 ZZ domain in complex with histone H3K4ac peptide

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