1ofc
From Proteopedia
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| - | [[Image:1ofc.gif|left|200px]] | ||
| - | + | ==nucleosome recognition module of ISWI ATPase== | |
| - | + | <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. | 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<ref>PMID:14536084</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1ofc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Grune | + | [[Category: Grune T]] |
| - | [[Category: Muller | + | [[Category: Muller CW]] |
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Current revision
nucleosome recognition module of ISWI ATPase
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