2Y9Z

Chromatin Remodeling Factor ISW1a(del_ATPase) in DNA complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.60 Å
  • R-Value Free: 0.291 
  • R-Value Work: 0.283 
  • R-Value Observed: 0.283 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structure and Mechanism of the Chromatin Remodelling Factor Isw1A

Yamada, K.Frouws, T.D.Angst, B.Fitzgerald, D.J.Deluca, C.Schimmele, K.Sargent, D.F.Richmond, T.J.

(2011) Nature 472: 448

  • DOI: https://doi.org/10.1038/nature09947
  • Primary Citation of Related Structures:  
    2Y9Y, 2Y9Z

  • 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'.


  • Organizational Affiliation

    ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20, CH-8093 Zürich, Switzerland.


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
IMITATION SWITCH PROTEIN 1 (DEL_ATPASE)374Saccharomyces cerevisiaeMutation(s): 0 
UniProt
Find proteins for P38144 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P38144 
Go to UniProtKB:  P38144
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP38144
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ISWI ONE COMPLEX PROTEIN 3624Saccharomyces cerevisiaeMutation(s): 0 
UniProt
Find proteins for P43596 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P43596 
Go to UniProtKB:  P43596
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP43596
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains LengthOrganismImage
I-DNA/E-DNA
C, D, E, F
48Saccharomyces cerevisiae
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.60 Å
  • R-Value Free: 0.291 
  • R-Value Work: 0.283 
  • R-Value Observed: 0.283 
  • Space Group: P 65 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 284.028α = 90
b = 284.028β = 90
c = 193.423γ = 120
Software Package:
Software NamePurpose
XDSdata reduction
SCALAdata scaling
HKL2MAPphasing
SHARPphasing
PHENIXrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-04-20
    Type: Initial release
  • Version 1.1: 2012-03-28
    Changes: Database references, Version format compliance