3WTP

Crystal Structure of the heterotypic nucleosome containing human CENP-A and H3.3

Summary for 3WTP

• Entry DOI: 10.2210/pdb3wtp/pdb
• Descriptor: Histone H3-like centromeric protein A, Histone H4, Histone H2A type 1-B/E, ... (6 entities in total)
• Functional Keywords: histone fold, dna binding, chromatin formation, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : P49450 P62805 P04908 P06899 P84243
• Total number of polymer chains: 10
• Total formula weight: 202808.05

Authors

Arimura, Y.,Shirayama, K.,Horikoshi, N.,Fujita, R.,Kagawa, W.,Fukagawa, T.,Almouzni, G.,Kurumizaka, H. (deposition date: 2014-04-14, release date: 2014-12-03, Last modification date: 2023-11-08)

Primary citation

Arimura, Y.,Shirayama, K.,Horikoshi, N.,Fujita, R.,Taguchi, H.,Kagawa, W.,Fukagawa, T.,Almouzni, G.,Kurumizaka, H.
Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3
Sci Rep, 4:7115-7115, 2014

PubMed Abstract: The centromere-specific histone H3 variant, CENP-A, is overexpressed in particular aggressive cancer cells, where it can be mislocalized ectopically in the form of heterotypic nucleosomes containing H3.3. In the present study, we report the crystal structure of the heterotypic CENP-A/H3.3 particle and reveal its "hybrid structure", in which the physical characteristics of CENP-A and H3.3 are conserved independently within the same particle. The CENP-A/H3.3 nucleosome forms an unexpectedly stable structure as compared to the CENP-A nucleosome, and allows the binding of the essential centromeric protein, CENP-C, which is ectopically mislocalized in the chromosomes of CENP-A overexpressing cells.

PubMed: 25408271
DOI: 10.1038/srep07115

Experimental method

X-RAY DIFFRACTION (2.67 Å)