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| | <StructureSection load='6j6t' size='340' side='right'caption='[[6j6t]], [[Resolution|resolution]] 2.36Å' scene=''> | | <StructureSection load='6j6t' size='340' side='right'caption='[[6j6t]], [[Resolution|resolution]] 2.36Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6j6t]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J6T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6J6T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6j6t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J6T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.36Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDA15, At3g18520, MYF24_23 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </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=6j6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j6t OCA], [https://pdbe.org/6j6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j6t RCSB], [https://www.ebi.ac.uk/pdbsum/6j6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j6t ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6j6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j6t OCA], [http://pdbe.org/6j6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j6t RCSB], [http://www.ebi.ac.uk/pdbsum/6j6t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j6t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HDA15_ARATH HDA15_ARATH]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). | + | [https://www.uniprot.org/uniprot/HDA15_ARATH HDA15_ARATH] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). |
| | <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> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Histone deacetylase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cheng, Y S]] | + | [[Category: Cheng YS]] |
| - | [[Category: Hsu, J C]] | + | [[Category: Hsu JC]] |
| - | [[Category: Hung, H C]] | + | [[Category: Hung HC]] |
| - | [[Category: Liu, T C]] | + | [[Category: Liu TC]] |
| - | [[Category: Arabidopsis]]
| + | |
| - | [[Category: Gene regulation]]
| + | |
| Structural highlights
Function
HDA15_ARATH Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity).
Publication Abstract from PubMed
Mammalian histone deacetylases (HDACs) undergo phosphorylation to regulate their localization, activity, and function. However, little is known about the regulation of plant HDAC function and activity by phosphorylation. Here, we report the crystal structure of the Reduced Potassium Dependency3/Histone Deacetylase1 (RPD3/HDA1) type class II histone deacetylase HDA15 in Arabidopsis (Arabidopsis thaliana). The histone deacetylase domain of HDA15 (HDA15HD) assembles as tetrameric forms with each monomer composed of 12 alpha-helices and 9 beta-sheets. The L1 loop and beta2 sheet of HDA15HD are the essential interfaces for the tetramer formation. The N-terminal zinc finger domain enhances HDA15HD dimerization and increases its enzymatic activity. Furthermore, HDA15 can also be phosphorylated at Ser-448 and Ser-452 in etiolated seedlings. The HDA15 phosphorylation status determines its subnuclear localization and oligomerization. Phosphomimetics of HDA15 partially disrupt its oligomerization and cause loss of enzymatic activity and translocation from the nucleolus into nucleoplasm. Together, these data indicate that phosphorylation plays a critical role in regulating the structure and function of HDA15.
Structure of Arabidopsis HISTONE DEACETYLASE15.,Chen CY, Tu YT, Hsu JC, Hung HC, Liu TC, Lee YH, Chou CC, Cheng YS, Wu K Plant Physiol. 2020 Nov;184(3):1585-1600. doi: 10.1104/pp.20.00604. Epub 2020 Sep, 2. PMID:32878973[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chen CY, Tu YT, Hsu JC, Hung HC, Liu TC, Lee YH, Chou CC, Cheng YS, Wu K. Structure of Arabidopsis HISTONE DEACETYLASE15. Plant Physiol. 2020 Nov;184(3):1585-1600. doi: 10.1104/pp.20.00604. Epub 2020 Sep, 2. PMID:32878973 doi:http://dx.doi.org/10.1104/pp.20.00604
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