Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI

Mol Cell. 2003 Aug;12(2):449-60. doi: 10.1016/s1097-2765(03)00273-9.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / metabolism*
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Chromatin / metabolism
  • Crystallography, X-Ray
  • Drosophila melanogaster / metabolism
  • Gene Deletion
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleosomes / metabolism*
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Proto-Oncogene Proteins c-myb / metabolism
  • Sequence Homology, Amino Acid
  • Time Factors
  • Transcription Factors / metabolism*


  • Chromatin
  • ISWI protein
  • Nucleosomes
  • Proto-Oncogene Proteins c-myb
  • Transcription Factors
  • Adenosine Triphosphatases

Associated data

  • PDB/1OFC