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2Y9Z

Chromatin Remodeling Factor ISW1a(del_ATPase) in DNA complex

Summary for 2Y9Z
Entry DOI10.2210/pdb2y9z/pdb
Related2Y9Y
DescriptorIMITATION SWITCH PROTEIN 1 (DEL_ATPASE), ISWI ONE COMPLEX PROTEIN 3, I-DNA/E-DNA (3 entities in total)
Functional Keywordstranscription, nuclear protein-dna complex, chromatin remodeling, nucleosome remodeling
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
More
Cellular locationNucleus: P38144 P43596
Total number of polymer chains6
Total formula weight175888.38
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 citationYamada, 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: 21525927
DOI: 10.1038/NATURE09947
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.601 Å)
Structure validation

237735

数据于2025-06-18公开中

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