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3W99

Crystal Structure of Human Nucleosome Core Particle lacking H4 N-terminal region

Summary for 3W99
Entry DOI10.2210/pdb3w99/pdb
Related3AFA 3W96 3W97 3W98
DescriptorHistone H3.1, Histone H4, Histone H2A type 1-B/E, ... (6 entities in total)
Functional Keywordsprotein-dna complex, histone-fold, nucleosome, structural protein-dna complex, structural protein/dna
Biological sourceHomo sapiens (Human)
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Total number of polymer chains10
Total formula weight202670.12
Authors
Iwasaki, W.,Miya, Y.,Horikoshi, N.,Osakabe, A.,Tachiwana, H.,Shibata, T.,Kagawa, W.,Kurumizaka, H. (deposition date: 2013-04-01, release date: 2013-08-28, Last modification date: 2023-11-08)
Primary citationIwasaki, W.,Miya, Y.,Horikoshi, N.,Osakabe, A.,Taguchi, H.,Tachiwana, H.,Shibata, T.,Kagawa, W.,Kurumizaka, H.
Contribution of histone N-terminal tails to the structure and stability of nucleosomes
FEBS Open Bio, 3:363-369, 2013
Cited by
PubMed Abstract: Histones are the protein components of the nucleosome, which forms the basic architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed of two common regions, the "histone fold" and the "histone tail". Many efforts have been focused on the mechanisms by which the post-translational modifications of histone tails regulate the higher-order chromatin architecture. On the other hand, previous biochemical studies have suggested that histone tails also affect the structure and stability of the nucleosome core particle itself. However, the precise contributions of each histone tail are unclear. In the present study, we determined the crystal structures of four mutant nucleosomes, in which one of the four histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N-terminal tail affected histone-DNA interactions and substantially decreased nucleosome stability. These findings provide important information for understanding the complex roles of histone tails in regulating chromatin structure.
PubMed: 24251097
DOI: 10.1016/j.fob.2013.08.007
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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