3AV2

The human nucleosome structure containing the histone variant H3.3

Summary for 3AV2

• Entry DOI: 10.2210/pdb3av2/pdb
• Descriptor: Histone H3.3, Histone H4, Histone H2A type 1-B/E, ... (6 entities in total)
• Functional Keywords: histone-fold, dna-binding protein, structural protein-dna complex, structural protein/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P84243 P62805 P04908 P06899
• Total number of polymer chains: 10
• Total formula weight: 202078.32

Authors

Tachiwana, H.,Osakabe, A.,Shiga, T.,Miya, M.,Kimura, H.,Kagawa, W.,Kurumizaka, H. (deposition date: 2011-02-18, release date: 2011-06-01, Last modification date: 2023-11-01)

Primary citation

Tachiwana, H.,Osakabe, A.,Shiga, T.,Miya, Y.,Kimura, H.,Kagawa, W.,Kurumizaka, H.
Structures of human nucleosomes containing major histone H3 variants
Acta Crystallogr.,Sect.D, 67:578-583, 2011

PubMed Abstract: The nucleosome is the fundamental repeating unit of chromatin, via which genomic DNA is packaged into the nucleus in eukaryotes. In the nucleosome, two copies of each core histone, H2A, H2B, H3 and H4, form a histone octamer which wraps 146 base pairs of DNA around itself. All of the core histones except for histone H4 have nonallelic isoforms called histone variants. In humans, eight histone H3 variants, H3.1, H3.2, H3.3, H3T, H3.5, H3.X, H3.Y and CENP-A, have been reported to date. Previous studies have suggested that histone H3 variants possess distinct functions in the formation of specific chromosome regions and/or in the regulation of transcription and replication. H3.1, H3.2 and H3.3 are the most abundant H3 variants. Here, crystal structures of human nucleosomes containing either H3.2 or H3.3 have been solved. The structures were essentially the same as that of the H3.1 nucleosome. Since the amino-acid residues specific for H3.2 and H3.3 are located on the accessible surface of the H3/H4 tetramer, they may be potential interaction sites for H3.2- and H3.3-specific chaperones.

PubMed: 21636898
DOI: 10.1107/S0907444911014818

Experimental method

X-RAY DIFFRACTION (2.8 Å)