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| | <StructureSection load='5j8j' size='340' side='right'caption='[[5j8j]], [[Resolution|resolution]] 2.72Å' scene=''> | | <StructureSection load='5j8j' size='340' side='right'caption='[[5j8j]], [[Resolution|resolution]] 2.72Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5j8j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J8J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5J8J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5j8j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J8J FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDA1, YNL021W, N2819 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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]] 2.716Å</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=5j8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8j OCA], [https://pdbe.org/5j8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j8j RCSB], [https://www.ebi.ac.uk/pdbsum/5j8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j8j 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=5j8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8j OCA], [http://pdbe.org/5j8j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j8j RCSB], [http://www.ebi.ac.uk/pdbsum/5j8j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j8j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HDA1_YEAST HDA1_YEAST]] 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. | + | [https://www.uniprot.org/uniprot/HDA1_YEAST HDA1_YEAST] 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. |
| | <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: Baker's yeast]] | |
| - | [[Category: Histone deacetylase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, X]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Shen, H]] | + | [[Category: Li X]] |
| - | [[Category: Teng, M]] | + | [[Category: Shen H]] |
| - | [[Category: Zhu, Y]] | + | [[Category: Teng M]] |
| - | [[Category: Deacetylase]]
| + | [[Category: Zhu Y]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
HDA1_YEAST 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.
Publication Abstract from PubMed
Hda1 is the catalytic core component of the H2B- and H3- specific histone deacetylase (HDAC) complex from Saccharomyces cerevisiae, which is involved in the epigenetic repression and plays a crucial role in transcriptional regulation and developmental events. Though the N-terminal catalytic HDAC domain of Hda1 is well characterized, the function of the C-terminal ARB2 domain remains unknown. In this study, we determine the crystal structure of the ARB2 domain from S. cerevisiae Hda1 at a resolution of 2.7 A. The ARB2 domain displays an alpha/beta sandwich architecture with an arm protruding outside. Two ARB2 domain molecules form a compact homo-dimer via the arm elements, and assemble as an inverse "V" shape. The pull-down and ITC results reveal that the ARB2 domain possesses the histone binding ability, recognizing both the H2A-H2B dimer and H3-H4 tetramer. Perturbation of the dimer interface abolishes the histone binding ability of the ARB2 domain, indicating that the unique dimer architecture of the ARB2 domain coincides with the function for anchoring to histone. Collectively, our data report the first structure of the ARB2 domain and disclose its histone binding ability, which is of benefit for understanding the deacetylation reaction catalyzed by the class II Hda1 HDAC complex.
Structural and histone binding ability characterization of the ARB2 domain of a histone deacetylase Hda1 from Saccharomyces cerevisiae.,Shen H, Zhu Y, Wang C, Yan H, Teng M, Li X Sci Rep. 2016 Sep 26;6:33905. doi: 10.1038/srep33905. PMID:27665728[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shen H, Zhu Y, Wang C, Yan H, Teng M, Li X. Structural and histone binding ability characterization of the ARB2 domain of a histone deacetylase Hda1 from Saccharomyces cerevisiae. Sci Rep. 2016 Sep 26;6:33905. doi: 10.1038/srep33905. PMID:27665728 doi:http://dx.doi.org/10.1038/srep33905
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