View source for 2bym


==Histone fold heterodimer of the Chromatin Accessibility Complex==
<StructureSection load='2bym' size='340' side='right'caption='[[2bym]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bym]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BYM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></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=2bym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bym OCA], [https://pdbe.org/2bym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bym RCSB], [https://www.ebi.ac.uk/pdbsum/2bym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bym ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CHRC_DROME CHRC_DROME] Histone-like protein which promotes nucleosome sliding of ATP-dependent nucleosome remodeling complexes (PubMed:10856248, PubMed:11447119). Part of the chromatin-accessibility complex (CHRAC) which uses energy/ATP to increase the general accessibility of DNA in chromatin (PubMed:10856248, PubMed:11447119). As an heterodimer with Chrac-14, binds DNA and facilitates nucleosome sliding by Acf (PubMed:16260604). As part of the CHRAC complex, required for oogenesis (PubMed:26851213).<ref>PMID:10856248</ref> <ref>PMID:11447119</ref> <ref>PMID:16260604</ref> <ref>PMID:26851213</ref> 
== 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/by/2bym_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=2bym ConSurf].
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== Publication Abstract from PubMed ==
The chromatin accessibility complex (CHRAC) is an abundant, evolutionarily conserved nucleosome remodeling machinery able to catalyze histone octamer sliding on DNA. CHRAC differs from the related ACF complex by the presence of two subunits with molecular masses of 14 and 16 kDa, whose structure and function were not known. We determined the structure of Drosophila melanogaster CHRAC14-CHRAC16 by X-ray crystallography at 2.4-angstroms resolution and found that they dimerize via a variant histone fold in a typical handshake structure. In further analogy to histones, CHRAC14-16 contain unstructured N- and C-terminal tail domains that protrude from the handshake structure. A dimer of CHRAC14-16 can associate with the N terminus of ACF1, thereby completing CHRAC. Low-affinity interactions of CHRAC14-16 with DNA significantly improve the efficiency of nucleosome mobilization by limiting amounts of ACF. Deletion of the negatively charged C terminus of CHRAC16 enhances DNA binding 25-fold but leads to inhibition of nucleosome sliding, in striking analogy to the effect of the DNA chaperone HMGB1 on nucleosome sliding. The presence of a surface compatible with DNA interaction and the geometry of an H2A-H2B heterodimer may provide a transient acceptor site for DNA dislocated from the histone surface and therefore facilitate the nucleosome remodeling process.

The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions.,Hartlepp KF, Fernandez-Tornero C, Eberharter A, Grune T, Muller CW, Becker PB Mol Cell Biol. 2005 Nov;25(22):9886-96. PMID:16260604<ref>PMID:16260604</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2bym" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Becker PB]]
[[Category: Eberharter A]]
[[Category: Fernandez-Tornero C]]
[[Category: Grune T]]
[[Category: Hartlepp KF]]
[[Category: Muller CW]]