4qqg

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==Crystal structure of an N-terminal HTATIP fragment==
==Crystal structure of an N-terminal HTATIP fragment==
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<StructureSection load='4qqg' size='340' side='right' caption='[[4qqg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='4qqg' size='340' side='right'caption='[[4qqg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qqg]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QQG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4qqg]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QQG 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=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KAT5, HTATIP, TIP60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4qqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqg OCA], [https://pdbe.org/4qqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qqg RCSB], [https://www.ebi.ac.uk/pdbsum/4qqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qqg ProSAT]</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=4qqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqg OCA], [http://pdbe.org/4qqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qqg RCSB], [http://www.ebi.ac.uk/pdbsum/4qqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qqg ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KAT5_HUMAN KAT5_HUMAN]] Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2.<ref>PMID:12776177</ref> <ref>PMID:15310756</ref> <ref>PMID:14966270</ref> <ref>PMID:15121871</ref> <ref>PMID:15042092</ref> <ref>PMID:16141325</ref> <ref>PMID:16387653</ref> <ref>PMID:17996965</ref> <ref>PMID:19909775</ref> <ref>PMID:24463511</ref>
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[https://www.uniprot.org/uniprot/KAT5_HUMAN KAT5_HUMAN] Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2.<ref>PMID:12776177</ref> <ref>PMID:15310756</ref> <ref>PMID:14966270</ref> <ref>PMID:15121871</ref> <ref>PMID:15042092</ref> <ref>PMID:16141325</ref> <ref>PMID:16387653</ref> <ref>PMID:17996965</ref> <ref>PMID:19909775</ref> <ref>PMID:24463511</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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The mixed-lineage leukemia (MLL)-AF10 fusion oncoprotein recruits DOT1L to the homeobox A (HOXA) gene cluster through its octapeptide motif leucine zipper (OM-LZ), thereby inducing and maintaining the MLL-AF10-associated leukemogenesis. However, the recognition mechanism between DOT1L and MLL-AF10 is unclear. Here, we present the crystal structures of both apo AF10(OM-LZ) and its complex with the coiled-coil domain of DOT1L. Disruption of the DOT1L-AF10 interface abrogates MLL-AF10-associated leukemic transformation. We further show that zinc stabilizes the DOT1L-AF10 complex and may be involved in the regulation of the HOXA gene expression. Our studies may also pave the way for the rational design of therapeutic drugs against MLL-rearranged leukemia.
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Tat-interactive protein 60 consists of an N-terminal chromo barrel domain (TIP60-CB) and a C-terminal acetyltransferase domain and acetylates histone and nonhistone proteins in diverse cellular processes. While TIP60-CB is thought to recognize histone tails, molecular details of this interaction remain unclear. Here, we attempted a quantitative analysis of the interaction between the human TIP60-CB and histone peptides, but did not observe any detectable binding by either fluorescence polarization or isothermal titration calorimetry assays. We also determined the crystal structure of the TIP60-CB alone. Analysis of the apo-structure reveals a putative peptide-binding site that might be occluded by the basic side chain of a residue in a unique beta hairpin between the two N-terminal strands of the beta barrel, leading to the inability of TIP60-CB to bind histones.
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Structural and functional analysis of the DOT1L-AF10 complex reveals mechanistic insights into MLL-AF10-associated leukemogenesis.,Zhang H, Zhou B, Qin S, Xu J, Harding R, Tempel W, Nayak V, Li Y, Loppnau P, Dou Y, Min J Genes Dev. 2018 Mar 1;32(5-6):341-346. doi: 10.1101/gad.311639.118. Epub 2018 Mar, 21. PMID:29563185<ref>PMID:29563185</ref>
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Structural and histone binding studies of the chromo barrel domain of TIP60.,Zhang Y, Lei M, Yang X, Feng Y, Yang Y, Loppnau P, Li Y, Yang Y, Min J, Liu Y FEBS Lett. 2018 Apr;592(7):1221-1232. doi: 10.1002/1873-3468.13021. Epub 2018 Mar, 25. PMID:29494751<ref>PMID:29494751</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==
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*[[Histone acetyltransferase|Histone acetyltransferase]]
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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: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Dobrovetsky, E]]
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[[Category: Dobrovetsky E]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Liu, Y]]
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[[Category: Liu Y]]
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[[Category: Min, J]]
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[[Category: Min J]]
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[[Category: Structural genomic]]
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[[Category: Tempel W]]
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[[Category: Tempel, W]]
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[[Category: Wernimont AK]]
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[[Category: Wernimont, A K]]
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[[Category: Sgc]]
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[[Category: Transferase]]
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Current revision

Crystal structure of an N-terminal HTATIP fragment

PDB ID 4qqg

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