3C1C

The effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin structure

Summary for 3C1C

• Entry DOI: 10.2210/pdb3c1c/pdb
• Related: 1AOI 1KX3 1KX5 1ZLA 1f66 1kx4 3C1B
• Descriptor: Histone H3-like, Histone H4, Histone H2A type 1, ... (6 entities in total)
• Functional Keywords: nucleosome, chromatin, histone h3, trimethylation, histone modification, nucleosomal surface, nucleosomal array, acetylation, chromosomal protein, dna-binding, methylation, nucleosome core, nucleus, phosphoprotein, ubl conjugation, structural protein-dna complex, structural protein/dna
• Biological source: Xenopus laevis (clawed frog,common platanna,platanna); More
• Cellular location: Nucleus: P02302 P62799 P06897; Nucleus (By similarity): Q28D68
• Total number of polymer chains: 10
• Total formula weight: 198902.65

Authors

Lu, X.,Simon, M.,Chodaparambil, J.,Hansen, J.,Shokat, K.,Luger, K. (deposition date: 2008-01-22, release date: 2008-10-07, Last modification date: 2024-11-13)

Primary citation

Lu, X.,Simon, M.D.,Chodaparambil, J.V.,Hansen, J.C.,Shokat, K.M.,Luger, K.
The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure.
Nat.Struct.Mol.Biol., 15:1122-1124, 2008

PubMed Abstract: Histone methylation regulates chromatin function dependent on the site and degree of the modification. In addition to creating binding sites for proteins, methylated lysine residues are likely to influence chromatin structure directly. Here we present crystal structures of nucleosomes reconstituted with methylated histones and investigate the folding behavior of resulting arrays. We demonstrate that dimethylation of histone H3 at lysine residue 79 locally alters the nucleosomal surface, whereas trimethylation of H4 at lysine residue 20 affects higher-order structure.

PubMed: 18794842
DOI: 10.1038/nsmb.1489

Experimental method

X-RAY DIFFRACTION (3.15 Å)