3q35

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<StructureSection load='3q35' size='340' side='right'caption='[[3q35]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='3q35' size='340' side='right'caption='[[3q35]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3q35]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q35 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3q35]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q35 FirstGlance]. <br>
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</td></tr><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=EDO:1,2-ETHANEDIOL'>EDO</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]] 3.3&#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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3d35|3d35]], [[3dm7|3dm7]], [[3q33|3q33]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIM2, L1377, REM50, RTT109, YLL002W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), N0890, VPS75, YNL246W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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<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>
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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=3q35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q35 OCA], [https://pdbe.org/3q35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q35 RCSB], [https://www.ebi.ac.uk/pdbsum/3q35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q35 ProSAT]</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=3q35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q35 OCA], [https://pdbe.org/3q35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q35 RCSB], [https://www.ebi.ac.uk/pdbsum/3q35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q35 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/RT109_YEAST RT109_YEAST]] Required for acetylation of 'Lys-56' of histone H3 (H3K56ac) which occurs in S phase and disappears during G(2)/M phase of the cell cycle and is involved in transcription DNA repair process. H3K56 acetylation weakens of the interaction between the histone core and the surrounding DNA in the nucleosomal particle and drives chromatin disassembly. Involved in regulation of Ty1 transposition.<ref>PMID:11779788</ref> <ref>PMID:17046836</ref> <ref>PMID:17369253</ref> <ref>PMID:17690098</ref> <ref>PMID:17320445</ref> <ref>PMID:17272722</ref> <ref>PMID:17272723</ref> <ref>PMID:18577595</ref> <ref>PMID:18723682</ref> [[https://www.uniprot.org/uniprot/VPS75_YEAST VPS75_YEAST]] Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.<ref>PMID:12134085</ref> <ref>PMID:17320445</ref>
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[https://www.uniprot.org/uniprot/RT109_YEAST RT109_YEAST] Required for acetylation of 'Lys-56' of histone H3 (H3K56ac) which occurs in S phase and disappears during G(2)/M phase of the cell cycle and is involved in transcription DNA repair process. H3K56 acetylation weakens of the interaction between the histone core and the surrounding DNA in the nucleosomal particle and drives chromatin disassembly. Involved in regulation of Ty1 transposition.<ref>PMID:11779788</ref> <ref>PMID:17046836</ref> <ref>PMID:17369253</ref> <ref>PMID:17690098</ref> <ref>PMID:17320445</ref> <ref>PMID:17272722</ref> <ref>PMID:17272723</ref> <ref>PMID:18577595</ref> <ref>PMID:18723682</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>
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[[Category: Atcc 18824]]
 
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[[Category: Histone acetyltransferase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Marmorstein, R]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Meeth, K]]
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[[Category: Marmorstein R]]
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[[Category: Tang, Y]]
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[[Category: Meeth K]]
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[[Category: Yuan, H]]
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[[Category: Tang Y]]
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[[Category: Autoacetylation at rtt109 lys290]]
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[[Category: Yuan H]]
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[[Category: Nuclear]]
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[[Category: Rtt109:vps75=2:2 stoichiometry complex]]
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[[Category: Transferase-chaperone complex]]
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Revision as of 08:13, 6 December 2023

Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation

PDB ID 3q35

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