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| | <StructureSection load='2bym' size='340' side='right'caption='[[2bym]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='2bym' size='340' side='right'caption='[[2bym]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bym]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. 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> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2byk|2byk]]</div></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> | | <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> | | </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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Becker, P B]] | + | [[Category: Becker PB]] |
| - | [[Category: Eberharter, A]] | + | [[Category: Eberharter A]] |
| - | [[Category: Fernandez-Tornero, C]] | + | [[Category: Fernandez-Tornero C]] |
| - | [[Category: Grune, T]] | + | [[Category: Grune T]] |
| - | [[Category: Hartlepp, K F]] | + | [[Category: Hartlepp KF]] |
| - | [[Category: Muller, C W]] | + | [[Category: Muller CW]] |
| - | [[Category: Chrac-14]]
| + | |
| - | [[Category: Chrac-16]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna-binding protein]]
| + | |
| - | [[Category: Histone fold]]
| + | |
| - | [[Category: Nucleosome sliding]]
| + | |
| Structural highlights
Function
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).[1] [2] [3] [4]
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
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Corona DF, Eberharter A, Budde A, Deuring R, Ferrari S, Varga-Weisz P, Wilm M, Tamkun J, Becker PB. Two histone fold proteins, CHRAC-14 and CHRAC-16, are developmentally regulated subunits of chromatin accessibility complex (CHRAC). EMBO J. 2000 Jun 15;19(12):3049-59. PMID:10856248 doi:10.1093/emboj/19.12.3049
- ↑ Eberharter A, Ferrari S, Längst G, Straub T, Imhof A, Varga-Weisz P, Wilm M, Becker PB. Acf1, the largest subunit of CHRAC, regulates ISWI-induced nucleosome remodelling. EMBO J. 2001 Jul 16;20(14):3781-8. PMID:11447119 doi:10.1093/emboj/20.14.3781
- ↑ Hartlepp KF, Fernandez-Tornero C, Eberharter A, Grune T, Muller CW, Becker PB. The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions. Mol Cell Biol. 2005 Nov;25(22):9886-96. PMID:16260604 doi:25/22/9886
- ↑ Börner K, Jain D, Vazquez-Pianzola P, Vengadasalam S, Steffen N, Fyodorov DV, Tomancak P, Konev A, Suter B, Becker PB. A role for tuned levels of nucleosome remodeler subunit ACF1 during Drosophila oogenesis. Dev Biol. 2016 Mar 15;411(2):217-230. PMID:26851213 doi:10.1016/j.ydbio.2016.01.039
- ↑ Hartlepp KF, Fernandez-Tornero C, Eberharter A, Grune T, Muller CW, Becker PB. The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions. Mol Cell Biol. 2005 Nov;25(22):9886-96. PMID:16260604 doi:25/22/9886
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