5j9w

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==Crystal structure of the NuA4 core complex==
==Crystal structure of the NuA4 core complex==
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<StructureSection load='5j9w' size='340' side='right' caption='[[5j9w]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='5j9w' size='340' side='right'caption='[[5j9w]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5j9w]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J9W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J9W FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5j9w]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J9W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J9W 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=ACO:ACETYL+COENZYME+*A'>ACO</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">X-ray diffraction, [[Resolution|Resolution]] 2.8&#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=ALY:N(6)-ACETYLLYSINE'>ALY</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=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5j9u|5j9u]], [[5j9t|5j9t]], [[5j9q|5j9q]]</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=5j9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j9w OCA], [https://pdbe.org/5j9w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j9w RCSB], [https://www.ebi.ac.uk/pdbsum/5j9w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j9w ProSAT]</span></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_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </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=5j9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j9w OCA], [http://pdbe.org/5j9w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j9w RCSB], [http://www.ebi.ac.uk/pdbsum/5j9w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j9w ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/YNG2_YEAST YNG2_YEAST]] Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in cell cycle progression and meiosis.<ref>PMID:10805724</ref> <ref>PMID:11544250</ref> <ref>PMID:11604499</ref> <ref>PMID:12417725</ref> [[http://www.uniprot.org/uniprot/ESA1_YEAST ESA1_YEAST]] Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me.<ref>PMID:9858608</ref> <ref>PMID:10082517</ref> <ref>PMID:10835360</ref> <ref>PMID:10911987</ref> <ref>PMID:12353039</ref> <ref>PMID:15175650</ref> <ref>PMID:15494307</ref> <ref>PMID:15045029</ref> <ref>PMID:15923609</ref> [[http://www.uniprot.org/uniprot/EPL1_YEAST EPL1_YEAST]] Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in gene silencing by neighboring heterochromatin, blockage of the silencing spreading along the chromosome, and required for cell cycle progression through G2/M.<ref>PMID:10911987</ref> <ref>PMID:12782659</ref> <ref>PMID:14966276</ref> <ref>PMID:15045029</ref> [[http://www.uniprot.org/uniprot/EAF6_YEAST EAF6_YEAST]] Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Component of the NuA3 histone acetyltransferase complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation.<ref>PMID:17157260</ref>
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[https://www.uniprot.org/uniprot/ESA1_YEAST ESA1_YEAST] Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me.<ref>PMID:9858608</ref> <ref>PMID:10082517</ref> <ref>PMID:10835360</ref> <ref>PMID:10911987</ref> <ref>PMID:12353039</ref> <ref>PMID:15175650</ref> <ref>PMID:15494307</ref> <ref>PMID:15045029</ref> <ref>PMID:15923609</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5j9w" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5j9w" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Histone acetyltransferase]]
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[[Category: Large Structures]]
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[[Category: Chen, Z C]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Xu, P]]
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[[Category: Chen ZC]]
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[[Category: Acetylation]]
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[[Category: Xu P]]
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[[Category: Histone]]
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[[Category: Nua4]]
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[[Category: Nucleosome]]
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[[Category: Transferase]]
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Current revision

Crystal structure of the NuA4 core complex

PDB ID 5j9w

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