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2byk

From Proteopedia

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Histone fold heterodimer of the Chromatin Accessibility Complex

Structural highlights

2byk is a 4 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DPOE3_DROME Accessory component of the DNA polymerase epsilon complex (By similarity). Participates in DNA repair and in chromosomal DNA replication (By similarity). Histone-like protein which promotes nucleosome sliding of ATP-dependent nucleosome remodeling complexes (PubMed:10856248, PubMed:11447119, PubMed:18327268). 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-16, binds DNA and facilitates nucleosome sliding by Acf (PubMed:16260604). Has a role in DNA damage response by preventing cid mislocalization to chromatin (PubMed:24703848).[UniProtKB:Q04603][UniProtKB:Q9NRF9]^[1] ^[2] ^[3] ^[4] ^[5]

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^[6]

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
↑ Suganuma T, Gutiérrez JL, Li B, Florens L, Swanson SK, Washburn MP, Abmayr SM, Workman JL. ATAC is a double histone acetyltransferase complex that stimulates nucleosome sliding. Nat Struct Mol Biol. 2008 Apr;15(4):364-72. PMID:18327268 doi:10.1038/nsmb.1397
↑ Mathew V, Pauleau AL, Steffen N, Bergner A, Becker PB, Erhardt S. The histone-fold protein CHRAC14 influences chromatin composition in response to DNA damage. Cell Rep. 2014 Apr 24;7(2):321-330. doi: 10.1016/j.celrep.2014.03.008. Epub 2014 , Apr 3. PMID:24703848 doi:http://dx.doi.org/10.1016/j.celrep.2014.03.008
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2byk"

@@ Line 1: / Line 1: @@
 ==Histone fold heterodimer of the Chromatin Accessibility Complex==
-<StructureSection load='2byk' size='340' side='right' caption='[[2byk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='2byk' size='340' side='right'caption='[[2byk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2byk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BYK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BYK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2byk]] 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=2BYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BYK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bym|2bym]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2byk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2byk OCA], [http://pdbe.org/2byk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2byk RCSB], [http://www.ebi.ac.uk/pdbsum/2byk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2byk 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=2byk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2byk OCA], [https://pdbe.org/2byk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2byk RCSB], [https://www.ebi.ac.uk/pdbsum/2byk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2byk ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/DPOE3_DROME DPOE3_DROME] Accessory component of the DNA polymerase epsilon complex (By similarity). Participates in DNA repair and in chromosomal DNA replication (By similarity). Histone-like protein which promotes nucleosome sliding of ATP-dependent nucleosome remodeling complexes (PubMed:10856248, PubMed:11447119, PubMed:18327268). 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-16, binds DNA and facilitates nucleosome sliding by Acf (PubMed:16260604). Has a role in DNA damage response by preventing cid mislocalization to chromatin (PubMed:24703848).[UniProtKB:Q04603][UniProtKB:Q9NRF9]<ref>PMID:10856248</ref> <ref>PMID:11447119</ref> <ref>PMID:16260604</ref> <ref>PMID:18327268</ref> <ref>PMID:24703848</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Drome]]
+[[Category: Drosophila melanogaster]]
-[[Category: Becker, P B]]
+[[Category: Large Structures]]
-[[Category: Eberharter, A]]
+[[Category: Becker PB]]
-[[Category: Fernandez-Tornero, C]]
+[[Category: Eberharter A]]
-[[Category: Grune, T]]
+[[Category: Fernandez-Tornero C]]
-[[Category: Hartlepp, K F]]
+[[Category: Grune T]]
-[[Category: Muller, C W]]
+[[Category: Hartlepp KF]]
-[[Category: Chrac-14]]
+[[Category: Muller CW]]
-[[Category: Chrac-16]]
-[[Category: Dna binding protein]]
-[[Category: Dna-binding protein]]
-[[Category: Histone fold]]
-[[Category: Nucleosome sliding]]

2byk

From Proteopedia

Current revision

Histone fold heterodimer of the Chromatin Accessibility Complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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