3qm0
From Proteopedia
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| - | [[Image:3qm0.png|left|200px]] | ||
| - | + | ==Crystal structure of RTT109-AC-CoA complex== | |
| + | <StructureSection load='3qm0' size='340' side='right'caption='[[3qm0]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3qm0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3d35 3d35]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QM0 FirstGlance]. <br> | ||
| + | </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=HG:MERCURY+(II)+ION'>HG</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">KIM2, L1377, REM50, RTT109, YLL002W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3qm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qm0 OCA], [https://pdbe.org/3qm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qm0 RCSB], [https://www.ebi.ac.uk/pdbsum/3qm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qm0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rtt109, also known as KAT11, is a recently characterized fungal-specific histone acetyltransferase (HAT) that modifies histone H3 lysine 56 (H3K56) to promote genome stability. Rtt109 does not show sequence conservation with other known HATs and depends on association with either of two histone chaperones, Asf1 or Vps75, for HAT activity. Here we report the X-ray crystal structure of an Rtt109-acetyl coenzyme A complex and carry out structure-based mutagenesis, combined with in vitro biochemical studies of the Rtt109-Vps75 complex and studies of Rtt109 function in vivo. The Rtt109 structure reveals noteworthy homology to the metazoan p300/CBP HAT domain but exhibits functional divergence, including atypical catalytic properties and mode of cofactor regulation. The structure reveals a buried autoacetylated lysine residue that we show is also acetylated in the Rtt109 protein purified from yeast cells. Implications for understanding histone substrate and chaperone binding by Rtt109 are discussed. | ||
| - | + | Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP.,Tang Y, Holbert MA, Wurtele H, Meeth K, Rocha W, Gharib M, Jiang E, Thibault P, Verreault A, Cole PA, Marmorstein R Nat Struct Mol Biol. 2008 Jul;15(7):738-45. Epub 2008 Jun 22. PMID:18568037<ref>PMID:18568037</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3qm0" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Histone acetyltransferase|Histone acetyltransferase]] | + | *[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Atcc 18824]] | ||
[[Category: Histone acetyltransferase]] | [[Category: Histone acetyltransferase]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Marmorstein, R | + | [[Category: Marmorstein, R]] |
| - | [[Category: Tang, Y | + | [[Category: Tang, Y]] |
[[Category: Auto-acetylation]] | [[Category: Auto-acetylation]] | ||
[[Category: Dna damage]] | [[Category: Dna damage]] | ||
[[Category: Dna repair]] | [[Category: Dna repair]] | ||
[[Category: Genome stability]] | [[Category: Genome stability]] | ||
| - | [[Category: Histone acetyltransferase]] | ||
[[Category: Histone h3 k56]] | [[Category: Histone h3 k56]] | ||
[[Category: Lys290]] | [[Category: Lys290]] | ||
Current revision
Crystal structure of RTT109-AC-CoA complex
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