2Y9Y
Chromatin Remodeling Factor ISW1a(del_ATPase)
Summary for 2Y9Y
| Entry DOI | 10.2210/pdb2y9y/pdb |
| Related | 2Y9Z |
| Descriptor | IMITATION SWITCH PROTEIN 1 (DEL_ATPASE), ISWI ONE COMPLEX PROTEIN 3 (2 entities in total) |
| Functional Keywords | transcription, nuclear protein complex, chromatin remodeling, nucleosome remodeling |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) More |
| Cellular location | Nucleus: P38144 P43596 |
| Total number of polymer chains | 2 |
| Total formula weight | 116777.50 |
| Authors | Yamada, K.,Frouws, T.D.,Angst, B.,Fitzgerald, D.J.,DeLuca, C.,Schimmele, K.,Sargent, D.F.,Richmond, T.J. (deposition date: 2011-02-17, release date: 2011-04-20, Last modification date: 2024-05-08) |
| Primary citation | Yamada, K.,Frouws, T.D.,Angst, B.,Fitzgerald, D.J.,Deluca, C.,Schimmele, K.,Sargent, D.F.,Richmond, T.J. Structure and Mechanism of the Chromatin Remodelling Factor Isw1A. Nature, 472:448-, 2011 Cited by PubMed Abstract: Site-specific recognition of DNA in eukaryotic organisms depends on the arrangement of nucleosomes in chromatin. In the yeast Saccharomyces cerevisiae, ISW1a and related chromatin remodelling factors are implicated in establishing the nucleosome repeat during replication and altering nucleosome position to affect gene activity. Here we have solved the crystal structures of S. cerevisiae ISW1a lacking its ATPase domain both alone and with DNA bound at resolutions of 3.25 Å and 3.60 Å, respectively, and we have visualized two different nucleosome-containing remodelling complexes using cryo-electron microscopy. The composite X-ray and electron microscopy structures combined with site-directed photocrosslinking analyses of these complexes suggest that ISW1a uses a dinucleosome substrate for chromatin remodelling. Results from a remodelling assay corroborate the dinucleosome model. We show how a chromatin remodelling factor could set the spacing between two adjacent nucleosomes acting as a 'protein ruler'. PubMed: 21525927DOI: 10.1038/NATURE09947 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.25 Å) |
Structure validation
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