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| | ==Solution structure of ZZZ3 ZZ domain in complex with histone H3K4ac peptide== | | ==Solution structure of ZZZ3 ZZ domain in complex with histone H3K4ac peptide== |
| - | <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]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <table><tr><td colspan='2'>[[6e86]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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='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=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6e83|6e83]]</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=6e86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e86 OCA], [https://pdbe.org/6e86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e86 RCSB], [https://www.ebi.ac.uk/pdbsum/6e86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e86 ProSAT]</span></td></tr> |
| - | <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> | + | |
| | </table> | | </table> |
| - | == 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> | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Kutateladze, T G]] | + | [[Category: Large Structures]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Kutateladze TG]] |
| - | [[Category: Chromatin]] | + | [[Category: Zhang Y]] |
| - | [[Category: Gene regulation]]
| + | |
| - | [[Category: Histone]]
| + | |
| - | [[Category: Zz domain]]
| + | |
| - | [[Category: Zzz3]]
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| Structural highlights
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mi W, Zhang Y, Lyu J, Wang X, Tong Q, Peng D, Xue Y, Tencer AH, Wen H, Li W, Kutateladze TG, Shi X. The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation. Nat Commun. 2018 Sep 14;9(1):3759. doi: 10.1038/s41467-018-06247-5. PMID:30217978 doi:http://dx.doi.org/10.1038/s41467-018-06247-5
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