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8KCC

Complex of DDM1-nucleosome(H2A.W) complex with DDM1 bound to SHL2

Summary for 8KCC
Entry DOI10.2210/pdb8kcc/pdb
EMDB information37099
DescriptorProbable histone H2A.7, Histone H2B.10, Histone H3.1, ... (9 entities in total)
Functional Keywordsddm1, nucleosome, h2a.w, structural protein
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains11
Total formula weight309220.63
Authors
Zhang, H.,Zhang, Y. (deposition date: 2023-08-07, release date: 2024-06-26, Last modification date: 2024-08-21)
Primary citationZhang, H.,Gu, Z.,Zeng, Y.,Zhang, Y.
Mechanism of heterochromatin remodeling revealed by the DDM1 bound nucleosome structures.
Structure, 32:1222-1230.e4, 2024
Cited by
PubMed Abstract: The SWI/SNF2 chromatin remodeling factor decreased DNA methylation 1 (DDM1) is essential for the silencing of transposable elements (TEs) in both euchromatic and heterochromatic regions. Here, we determined the cryo-EM structures of DDM1-nucleosome and DDM1-nucleosome complexes at near-atomic resolution in the presence of the ATP analog ADP-BeFx. The structures show that nucleosomal DNA is unwrapped more on the surface of the histone octamer containing histone H2A than that containing histone H2A.W. DDM1 embraces one DNA gyre of the nucleosome and interacts with the N-terminal tails of histone H4. Although we did not observe DDM1-H2A.W interactions in our structures, the results of the pull-down experiments suggest a direct interaction between DDM1 and the core region of histone H2A.W. Our work provides mechanistic insights into the heterochromatin remodeling process driven by DDM1 in plants.
PubMed: 38870940
DOI: 10.1016/j.str.2024.05.013
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

227344

数据于2024-11-13公开中

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