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| - | [[Image:1ofc.gif|left|200px]]<br /><applet load="1ofc" size="350" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1ofc, resolution 1.90Å" /> | |
| - | '''NUCLEOSOME RECOGNITION MODULE OF ISWI ATPASE'''<br /> | |
| | | | |
| - | ==Overview== | + | ==nucleosome recognition module of ISWI ATPase== |
| - | Energy-dependent nucleosome remodeling emerges as a key process endowing, chromatin with dynamic properties. However, the principles by which, remodeling ATPases interact with their nucleosome substrate to alter, histone-DNA interactions are only poorly understood. We have identified a, substrate recognition domain in the C-terminal half of the remodeling, ATPase ISWI and determined its structure by X-ray crystallography. The, structure comprises three domains, a four-helix domain with a novel fold, and two alpha-helical domains related to the modules of c-Myb, SANT and, SLIDE, which are linked by a long helix. An integrated structural and, functional analysis of these domains provides insight into how ISWI, interacts with the nucleosomal substrate. | + | <StructureSection load='1ofc' size='340' side='right'caption='[[1ofc]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[1ofc]] is a 1 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=1OFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OFC 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]] 1.9Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G4D:4-DEOXY-ALPHA-D-GLUCOSE'>G4D</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1ofc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ofc OCA], [https://pdbe.org/1ofc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ofc RCSB], [https://www.ebi.ac.uk/pdbsum/1ofc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ofc ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ISWI_DROME ISWI_DROME] Energy-transducing component of the chromatin-remodeling complexes NURF (nucleosome-remodeling factor), ACF (ATP-utilizing chromatin assembly and remodeling factor), and CHRAC (chromatin accessibility complex) (PubMed:10856248, PubMed:11447119). NURF catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. It is required for homeotic gene expression, proper larval blood cell development, normal male X chromosome morphology, ecdysteroid signaling and metamorphosis (PubMed:12502740, PubMed:16264191, PubMed:8521501, PubMed:8521502).<ref>PMID:10856248</ref> <ref>PMID:11447119</ref> <ref>PMID:12502740</ref> <ref>PMID:16264191</ref> <ref>PMID:8521501</ref> <ref>PMID:8521502</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/of/1ofc_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=1ofc ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Energy-dependent nucleosome remodeling emerges as a key process endowing chromatin with dynamic properties. However, the principles by which remodeling ATPases interact with their nucleosome substrate to alter histone-DNA interactions are only poorly understood. We have identified a substrate recognition domain in the C-terminal half of the remodeling ATPase ISWI and determined its structure by X-ray crystallography. The structure comprises three domains, a four-helix domain with a novel fold and two alpha-helical domains related to the modules of c-Myb, SANT and SLIDE, which are linked by a long helix. An integrated structural and functional analysis of these domains provides insight into how ISWI interacts with the nucleosomal substrate. |
| | | | |
| - | ==About this Structure==
| + | Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.,Grune T, Brzeski J, Eberharter A, Clapier CR, Corona DF, Becker PB, Muller CW Mol Cell. 2003 Aug;12(2):449-60. PMID:14536084<ref>PMID:14536084</ref> |
| - | 1OFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=G4D:'>G4D</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+X'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OFC OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI., Grune T, Brzeski J, Eberharter A, Clapier CR, Corona DF, Becker PB, Muller CW, Mol Cell. 2003 Aug;12(2):449-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14536084 14536084]
| + | </div> |
| | + | <div class="pdbe-citations 1ofc" style="background-color:#fffaf0;"></div> |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Drosophila melanogaster]] | | [[Category: Drosophila melanogaster]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Grune, T.]] | + | [[Category: Grune T]] |
| - | [[Category: Muller, C.W.]] | + | [[Category: Muller CW]] |
| - | [[Category: G4D]]
| + | |
| - | [[Category: GLC]]
| + | |
| - | [[Category: GOL]]
| + | |
| - | [[Category: atpase]]
| + | |
| - | [[Category: chromatin remodeling factor]]
| + | |
| - | [[Category: iswi]]
| + | |
| - | [[Category: nucleosome recognition]]
| + | |
| - | [[Category: sant domain]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:57:23 2008''
| + | |
| Structural highlights
Function
ISWI_DROME Energy-transducing component of the chromatin-remodeling complexes NURF (nucleosome-remodeling factor), ACF (ATP-utilizing chromatin assembly and remodeling factor), and CHRAC (chromatin accessibility complex) (PubMed:10856248, PubMed:11447119). NURF catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. It is required for homeotic gene expression, proper larval blood cell development, normal male X chromosome morphology, ecdysteroid signaling and metamorphosis (PubMed:12502740, PubMed:16264191, PubMed:8521501, PubMed:8521502).[1] [2] [3] [4] [5] [6]
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
Energy-dependent nucleosome remodeling emerges as a key process endowing chromatin with dynamic properties. However, the principles by which remodeling ATPases interact with their nucleosome substrate to alter histone-DNA interactions are only poorly understood. We have identified a substrate recognition domain in the C-terminal half of the remodeling ATPase ISWI and determined its structure by X-ray crystallography. The structure comprises three domains, a four-helix domain with a novel fold and two alpha-helical domains related to the modules of c-Myb, SANT and SLIDE, which are linked by a long helix. An integrated structural and functional analysis of these domains provides insight into how ISWI interacts with the nucleosomal substrate.
Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI.,Grune T, Brzeski J, Eberharter A, Clapier CR, Corona DF, Becker PB, Muller CW Mol Cell. 2003 Aug;12(2):449-60. PMID:14536084[7]
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
- ↑ Badenhorst P, Voas M, Rebay I, Wu C. Biological functions of the ISWI chromatin remodeling complex NURF. Genes Dev. 2002 Dec 15;16(24):3186-98. PMID:12502740 doi:10.1101/gad.1032202
- ↑ Badenhorst P, Xiao H, Cherbas L, Kwon SY, Voas M, Rebay I, Cherbas P, Wu C. The Drosophila nucleosome remodeling factor NURF is required for Ecdysteroid signaling and metamorphosis. Genes Dev. 2005 Nov 1;19(21):2540-5. PMID:16264191 doi:10.1101/gad.1342605
- ↑ Tsukiyama T, Wu C. Purification and properties of an ATP-dependent nucleosome remodeling factor. Cell. 1995 Dec 15;83(6):1011-20. PMID:8521501 doi:10.1016/0092-8674(95)90216-3
- ↑ Tsukiyama T, Daniel C, Tamkun J, Wu C. ISWI, a member of the SWI2/SNF2 ATPase family, encodes the 140 kDa subunit of the nucleosome remodeling factor. Cell. 1995 Dec 15;83(6):1021-6. PMID:8521502 doi:10.1016/0092-8674(95)90217-1
- ↑ Grune T, Brzeski J, Eberharter A, Clapier CR, Corona DF, Becker PB, Muller CW. Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI. Mol Cell. 2003 Aug;12(2):449-60. PMID:14536084
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