Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8WHB

Structure of nucleosome core particle of Arabidopsis thaliana

Summary for 8WHB
Entry DOI10.2210/pdb8whb/pdb
EMDB information37538
DescriptorHistone H3.1, Histone H4, Histone H2A.6, ... (6 entities in total)
Functional Keywordsnucleosome, chromatin, histone, protein dna interaction, nucleoprotein, gene regulation
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains10
Total formula weight204535.30
Authors
Liu, Y.,Zhang, Z.,Du, J. (deposition date: 2023-09-23, release date: 2024-04-17, Last modification date: 2025-07-16)
Primary citationLiu, Y.,Zhang, Z.,Hu, H.,Chen, W.,Zhang, F.,Wang, Q.,Wang, C.,Yan, K.,Du, J.
Molecular basis of chromatin remodelling by DDM1 involved in plant DNA methylation.
Nat.Plants, 10:374-380, 2024
Cited by
PubMed Abstract: Eukaryotic gene regulation occurs at the chromatin level, which requires changing the chromatin structure by a group of ATP-dependent DNA translocases-namely, the chromatin remodellers. In plants, chromatin remodellers function in various biological processes and possess both conserved and plant-specific components. DECREASE IN DNA METHYLATION 1 (DDM1) is a plant chromatin remodeller that plays a key role in the maintenance DNA methylation. Here we determined the structures of Arabidopsis DDM1 in complex with nucleosome in ADP-BeF-bound, ADP-bound and nucleotide-free conformations. We show that DDM1 specifically recognizes the H4 tail and nucleosomal DNA. The conformational differences between ADP-BeF-bound, ADP-bound and nucleotide-free DDM1 suggest a chromatin remodelling cycle coupled to ATP binding, hydrolysis and ADP release. This, in turn, triggers conformational changes in the DDM1-bound nucleosomal DNA, which alters the nucleosome structure and promotes DNA sliding. Together, our data reveal the molecular basis of chromatin remodelling by DDM1.
PubMed: 38413824
DOI: 10.1038/s41477-024-01640-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.17 Å)
Structure validation

247035

PDB entries from 2026-01-07

PDB statisticsPDBj update infoContact PDBjnumon