1OFC
nucleosome recognition module of ISWI ATPase
Summary for 1OFC
| Entry DOI | 10.2210/pdb1ofc/pdb |
| Descriptor | ISWI PROTEIN, alpha-D-glucopyranose, 4-deoxy-alpha-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | nuclear protein, chromatin remodeling factor, iswi, atpase, sant domain, nucleosome recognition |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Total number of polymer chains | 1 |
| Total formula weight | 36322.18 |
| Authors | Grune, T.,Muller, C.W. (deposition date: 2003-04-10, release date: 2003-09-05, Last modification date: 2024-05-08) |
| Primary citation | Grune, T.,Brzeski, J.,Eberharter, A.,Clapier, C.R.,Corona, D.F.V.,Becker, P.B.,Muller, C.W. Crystal Structure and Functional Analysis of a Nucleosome Recognition Module of the Remodeling Factor Iswi Mol.Cell, 12:449-, 2003 Cited by PubMed Abstract: 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. PubMed: 14536084DOI: 10.1016/S1097-2765(03)00273-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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