7SWY

2.6 A structure of a 40-601[TA-rich+1]-40 nucleosome

Summary for 7SWY

• Entry DOI: 10.2210/pdb7swy/pdb
• EMDB information: 25479 25480 25481 25483
• Descriptor: Histone H3, Histone H4, Histone H2A, ... (6 entities in total)
• Functional Keywords: chd1, chromatin remodeling, atpase, dbd, nucleosome, remodeling, transcription, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 10
• Total formula weight: 247676.08

Authors

Nodelman, I.M.,Bowman, G.D.,Armache, J.-P. (deposition date: 2021-11-21, release date: 2022-03-02, Last modification date: 2024-06-05)

Primary citation

Nodelman, I.M.,Das, S.,Faustino, A.M.,Fried, S.D.,Bowman, G.D.,Armache, J.P.
Nucleosome recognition and DNA distortion by the Chd1 remodeler in a nucleotide-free state.
Nat.Struct.Mol.Biol., 29:121-129, 2022

PubMed Abstract: Chromatin remodelers are ATP-dependent enzymes that reorganize nucleosomes within all eukaryotic genomes. Here we report a complex of the Chd1 remodeler bound to a nucleosome in a nucleotide-free state, determined by cryo-EM to 2.3 Å resolution. The remodeler stimulates the nucleosome to absorb an additional nucleotide on each strand at two different locations: on the tracking strand within the ATPase binding site and on the guide strand one helical turn from the ATPase motor. Remarkably, the additional nucleotide on the tracking strand is associated with a local transformation toward an A-form geometry, explaining how sequential ratcheting of each DNA strand occurs. The structure also reveals a histone-binding motif, ChEx, which can block opposing remodelers on the nucleosome and may allow Chd1 to participate in histone reorganization during transcription.

PubMed: 35173352
DOI: 10.1038/s41594-021-00719-x

Experimental method

ELECTRON MICROSCOPY (2.6 Å)