3hgq

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{{Seed}}
 
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[[Image:3hgq.jpg|left|200px]]
 
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==Structural and functional studies of the yeast class II Hda1 HDAC complex==
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The line below this paragraph, containing "STRUCTURE_3hgq", creates the "Structure Box" on the page.
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<StructureSection load='3hgq' size='340' side='right'caption='[[3hgq]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3hgq]] is a 4 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=3HGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HGQ FirstGlance]. <br>
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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&#8491;</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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_3hgq| PDB=3hgq | SCENE= }}
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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=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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hg/3hgq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hgq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Structural and functional studies of the yeast class II Hda1 HDAC complex===
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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<ref>PMID:19573535</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3hgq" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19573535}}, adds the Publication Abstract to the page
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*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19573535 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19573535}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3HGQ is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HGQ OCA].
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==Reference==
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<ref group="xtra">PMID:19573535</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Lee, J H.]]
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[[Category: Lee JH]]
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[[Category: Maskos, K.]]
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[[Category: Maskos K]]
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[[Category: Chromatin regulator]]
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[[Category: Coiled coil]]
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[[Category: Nucleus]]
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[[Category: Reca-like domain]]
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[[Category: Repressor]]
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[[Category: Swi2/snf2 helical domain]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 19 13:15:13 2009''
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Current revision

Structural and functional studies of the yeast class II Hda1 HDAC complex

PDB ID 3hgq

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