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2ozu
From Proteopedia
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| - | [[Image:2ozu.jpg|left|200px]]<br /><applet load="2ozu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2ozu, resolution 2.30Å" /> | ||
| - | '''Crystal structure of human MYST histone acetyltransferase 3 in complex with acetylcoenzyme A'''<br /> | ||
| - | == | + | ==Crystal structure of human MYST histone acetyltransferase 3 in complex with acetylcoenzyme A== |
| - | + | <StructureSection load='2ozu' size='340' side='right'caption='[[2ozu]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2ozu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OZU FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACM:ACETAMIDE'>ACM</scene>, <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYST3, MOZ, RUNXBP2, ZNF220 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></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=2ozu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ozu OCA], [https://pdbe.org/2ozu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ozu RCSB], [https://www.ebi.ac.uk/pdbsum/2ozu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ozu ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | [ | + | == Disease == |
| - | [ | + | [[https://www.uniprot.org/uniprot/KAT6A_HUMAN KAT6A_HUMAN]] Note=Chromosomal aberrations involving KAT6A may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with CREBBP; translocation t(8;22)(p11;q13) with EP300. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation. Note=A chromosomal aberration involving KAT6A is a cause of therapy-related myelodysplastic syndrome. Translocation t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion protein. |
| - | [[ | + | == Function == |
| - | + | [[https://www.uniprot.org/uniprot/KAT6A_HUMAN KAT6A_HUMAN]] Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2.<ref>PMID:11742995</ref> <ref>PMID:11965546</ref> <ref>PMID:12771199</ref> <ref>PMID:16387653</ref> <ref>PMID:17925393</ref> | |
| - | [[ | + | == Evolutionary Conservation == |
| - | [[ | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oz/2ozu_consurf.spt"</scriptWhenChecked> | |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |
| - | [ | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | [[ | + | </jmolCheckbox> |
| - | [ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ozu ConSurf]. |
| - | + | <div style="clear:both"></div> | |
| - | + | ||
| - | + | ==See Also== | |
| + | *[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Histone acetyltransferase]] | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith, C H]] | ||
| + | [[Category: Bernstein, G]] | ||
| + | [[Category: Bochkarev, A]] | ||
| + | [[Category: Dombrovski, L]] | ||
| + | [[Category: Dong, A]] | ||
| + | [[Category: Edwards, A M]] | ||
| + | [[Category: Loppnau, P]] | ||
| + | [[Category: Min, J]] | ||
| + | [[Category: Plotnikov, A N]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Sundstrom, M]] | ||
| + | [[Category: Weigelt, J]] | ||
| + | [[Category: Wu, H]] | ||
| + | [[Category: Sgc]] | ||
| + | [[Category: Transferase]] | ||
Current revision
Crystal structure of human MYST histone acetyltransferase 3 in complex with acetylcoenzyme A
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