6G0L

Structure of two molecules of the chromatin remodelling enzyme Chd1 bound to a nucleosome

Summary for 6G0L

• Entry DOI: 10.2210/pdb6g0l/pdb
• EMDB information: 4318 4336
• Descriptor: Histone H3, BERYLLIUM TRIFLUORIDE ION, Histone H4, ... (10 entities in total)
• Functional Keywords: chromatin remodellers, motor protein
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 12
• Total formula weight: 556722.51

Authors

Sundaramoorthy, R.,Owen-hughes, T.,Norman, D.G.,Hughes, A. (deposition date: 2018-03-19, release date: 2018-08-22, Last modification date: 2018-11-21)

Primary citation

Sundaramoorthy, R.,Hughes, A.L.,El-Mkami, H.,Norman, D.G.,Ferreira, H.,Owen-Hughes, T.
Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome.
Elife, 7:-, 2018

PubMed Abstract: ATP-dependent chromatin remodelling proteins represent a diverse family of proteins that share ATPase domains that are adapted to regulate protein-DNA interactions. Here, we present structures of the Chd1 protein engaged with nucleosomes in the presence of the transition state mimic ADP-beryllium fluoride. The path of DNA strands through the ATPase domains indicates the presence of contacts conserved with single strand translocases and additional contacts with both strands that are unique to Snf2 related proteins. The structure provides connectivity between rearrangement of ATPase lobes to a closed, nucleotide bound state and the sensing of linker DNA. Two turns of linker DNA are prised off the surface of the histone octamer as a result of Chd1 binding, and both the histone H3 tail and ubiquitin conjugated to lysine 120 are re-orientated towards the unravelled DNA. This indicates how changes to nucleosome structure can alter the way in which histone epitopes are presented.

PubMed: 30079888
DOI: 10.7554/eLife.35720

Experimental method

ELECTRON MICROSCOPY (10 Å)