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7TN2

Composite model of a Chd1-nucleosome complex in the nucleotide-free state derived from 2.3A and 2.7A Cryo-EM maps

Summary for 7TN2
Entry DOI10.2210/pdb7tn2/pdb
EMDB information25479 25480
DescriptorHistone H3, Histone H4, Histone H2A type 1, ... (7 entities in total)
Functional Keywordschd1, chromatin remodeling, atpase, dbd, nucleosome, remodeling, transcription, dna binding protein
Biological sourceXenopus laevis (African clawed frog)
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Total number of polymer chains11
Total formula weight380981.33
Authors
Nodelman, I.M.,Bowman, G.D.,Armache, J.-P. (deposition date: 2022-01-20, release date: 2022-03-02, Last modification date: 2024-02-21)
Primary citationNodelman, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.3 Å)
Structure validation

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