1ofc
From Proteopedia
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|PDB= 1ofc |SIZE=350|CAPTION= <scene name='initialview01'>1ofc</scene>, resolution 1.90Å | |PDB= 1ofc |SIZE=350|CAPTION= <scene name='initialview01'>1ofc</scene>, resolution 1.90Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+X'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+X'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=G4D:4-DEOXY-ALPHA-D-GLUCOSE'>G4D</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ofc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ofc OCA], [http://www.ebi.ac.uk/pdbsum/1ofc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ofc RCSB]</span> | ||
}} | }} | ||
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[[Category: Grune, T.]] | [[Category: Grune, T.]] | ||
[[Category: Muller, C W.]] | [[Category: Muller, C W.]] | ||
| - | [[Category: G4D]] | ||
| - | [[Category: GLC]] | ||
| - | [[Category: GOL]] | ||
[[Category: atpase]] | [[Category: atpase]] | ||
[[Category: chromatin remodeling factor]] | [[Category: chromatin remodeling factor]] | ||
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[[Category: sant domain]] | [[Category: sant domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:44:29 2008'' |
Revision as of 19:44, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NUCLEOSOME RECOGNITION MODULE OF ISWI ATPASE
Overview
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
1OFC is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
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
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