Ontology highlight
ABSTRACT:
SUBMITTER: Sundaramoorthy R
PROVIDER: S-EPMC5391205 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
Sundaramoorthy Ramasubramanian R Hughes Amanda L AL Singh Vijender V Wiechens Nicola N Ryan Daniel P DP El-Mkami Hassane H Petoukhov Maxim M Svergun Dmitri I DI Treutlein Barbara B Quack Salina S Fischer Monika M Michaelis Jens J Böttcher Bettina B Norman David G DG Owen-Hughes Tom T
eLife 20170323
The yeast Chd1 protein acts to position nucleosomes across genomes. Here, we model the structure of the Chd1 protein in solution and when bound to nucleosomes. In the apo state, the DNA-binding domain contacts the edge of the nucleosome while in the presence of the non-hydrolyzable ATP analog, ADP-beryllium fluoride, we observe additional interactions between the ATPase domain and the adjacent DNA gyre 1.5 helical turns from the dyad axis of symmetry. Binding in this conformation involves unrave ...[more]