2aqe: Difference between revisions

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{{Seed}}
[[Image:2aqe.png|left|200px]]


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==Structural and functional analysis of ada2 alpha swirm domain==
The line below this paragraph, containing "STRUCTURE_2aqe", creates the "Structure Box" on the page.
<StructureSection load='2aqe' size='340' side='right'caption='[[2aqe]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2aqe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AQE FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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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=2aqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aqe OCA], [https://pdbe.org/2aqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aqe RCSB], [https://www.ebi.ac.uk/pdbsum/2aqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aqe ProSAT]</span></td></tr>
{{STRUCTURE_2aqe|  PDB=2aqe  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/TAD2A_MOUSE TAD2A_MOUSE] Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Required for the function of some acidic activation domains, which activate transcription from a distant site (By similarity). Binds double-stranded DNA. Binds dinucleosomes, probably at the linker region between neighboring nucleosomes. Plays a role in chromatin remodeling (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aq/2aqe_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2aqe ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The evolutionarily conserved Swi3p, Rsc8p and Moira (SWIRM) domain is found in many chromosomal proteins involved in chromatin modifications or remodeling. Here we report the three-dimensional solution structure of the SWIRM domain from the human transcriptional adaptor ADA2alpha. The structure reveals a five-helix bundle consisting of two helix-turn-helix motifs connected by a central long helix, reminiscent of the histone fold. Using structural and biochemical analyses, we showed that the SWIRM domains of human ADA2alpha and SMARC2 bind to double-stranded and nucleosomal DNA, and we identified amino acid residues required for this function. We demonstrated that the ADA2alpha SWIRM domain is colocalized with lysine-acetylated histone H3 in the cell nucleus and that it potentiates the ACF remodeling activity by enhancing accessibility of nucleosomal linker DNA bound to histone H1. These data suggest a functional role of the SWIRM domain in chromatin remodeling.


===Structural and functional analysis of ada2 alpha swirm domain===
Structure and chromosomal DNA binding of the SWIRM domain.,Qian C, Zhang Q, Li S, Zeng L, Walsh MJ, Zhou MM Nat Struct Mol Biol. 2005 Dec;12(12):1078-85. Epub 2005 Nov 20. PMID:16299514<ref>PMID:16299514</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_16299514}}, adds the Publication Abstract to the page
<div class="pdbe-citations 2aqe" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 16299514 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_16299514}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2AQE is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AQE OCA].
 
==Reference==
<ref group="xtra">PMID:16299514</ref><references group="xtra"/>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Qian, C.]]
[[Category: Qian C]]
[[Category: Zeng, L.]]
[[Category: Zeng L]]
[[Category: Zhang, Q.]]
[[Category: Zhang Q]]
[[Category: Zhou, M M.]]
[[Category: Zhou M-M]]
[[Category: Helix-turn-helix]]
 
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Retrieved from "https://proteopedia.org/2aqe"