|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Structural and functional studies of the yeast class II Hda1 HDAC complex== | | ==Structural and functional studies of the yeast class II Hda1 HDAC complex== |
| - | <StructureSection load='3hgq' size='340' side='right' caption='[[3hgq]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='3hgq' size='340' side='right'caption='[[3hgq]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hgq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HGQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hgq]] is a 4 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=3HGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HGQ FirstGlance]. <br> |
| | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hgt|3hgt]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hgt|3hgt]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDA3, PLO1, YPR179C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDA3, PLO1, YPR179C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hgq OCA], [http://pdbe.org/3hgq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hgq RCSB], [http://www.ebi.ac.uk/pdbsum/3hgq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hgq 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=3hgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hgq OCA], [https://pdbe.org/3hgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hgq RCSB], [https://www.ebi.ac.uk/pdbsum/3hgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hgq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HDA3_YEAST HDA3_YEAST]] Required for activity of HDA1 histone deacetylase complex. The HDA1 histone deacetylase complex is 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.<ref>PMID:8663039</ref> <ref>PMID:11287668</ref> | + | [[https://www.uniprot.org/uniprot/HDA3_YEAST HDA3_YEAST]] Required for activity of HDA1 histone deacetylase complex. The HDA1 histone deacetylase complex is 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.<ref>PMID:8663039</ref> <ref>PMID:11287668</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 32: |
Line 32: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Histone deacetylase|Histone deacetylase]] | + | *[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 38: |
Line 38: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Atcc 18824]] | | [[Category: Atcc 18824]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Huber, R]] | | [[Category: Huber, R]] |
| | [[Category: Lee, J H]] | | [[Category: Lee, J H]] |
| Structural highlights
Function
[HDA3_YEAST] Required for activity of HDA1 histone deacetylase complex. The HDA1 histone deacetylase complex is 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.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Yeast class II Hda1 histone deacetylase (HDAC) complex is an H2B- and H3-specific HDAC in Saccharomyces cerevisiae consisting of three previously identified subunits, the catalytic subunit scHda1p and two non-catalytic structural subunits scHda2p and scHda3p. We co-expressed and co-purified recombinant yeast class II HDAC complex from bacteria as a functionally active and trichostatin-A-sensitive hetero-tetrameric complex. According to an extensive analysis of domain organization and interaction of all subunits (or domains), the N-terminal domain of scHda1p associates through the C-terminal coiled-coil domains (CCDs) of the scHda2p-scHda3p sub-complex, yielding a truncated scHda1pHDAC-scHda2pCCD2-scHda3pCCD3 complex with indistinguishable deacetylase activity compared to the full-length complex in vitro. We characterized the interaction of the HDAC complex with either single-stranded or double-stranded DNA and identified the N-terminal halves of scHda2p and scHda3p as binding modules. A high-resolution structure of the scHda3p DNA-binding domain by X-ray crystallography is presented. The crystal structure shows an unanticipated structural homology with the C-terminal helicase lobes of SWI2/SNF2 chromatin-remodeling domains of the Rad54 family enzymes. DNA binding is unspecific for nucleotide sequence and structure, similar to the Rad54 enzymes in vitro. Our structural and functional analyses of the budding yeast class II Hda1 HDAC complex provide insight into DNA recognition and deacetylation of histones in nucleosomes.
Structural and functional studies of the yeast class II Hda1 histone deacetylase complex.,Lee JH, Maskos K, Huber R J Mol Biol. 2009 Aug 28;391(4):744-57. Epub 2009 Jun 30. PMID:19573535[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Carmen AA, Rundlett SE, Grunstein M. HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex. J Biol Chem. 1996 Jun 28;271(26):15837-44. PMID:8663039
- ↑ Wu J, Carmen AA, Kobayashi R, Suka N, Grunstein M. HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1. Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4391-6. Epub 2001 Apr 3. PMID:11287668 doi:http://dx.doi.org/10.1073/pnas.081560698
- ↑ Lee JH, Maskos K, Huber R. Structural and functional studies of the yeast class II Hda1 histone deacetylase complex. J Mol Biol. 2009 Aug 28;391(4):744-57. Epub 2009 Jun 30. PMID:19573535 doi:10.1016/j.jmb.2009.06.059
|
