Summary information and primary citation

PDB-id
3wtp; SNAP-derived features in text and JSON formats; DNAproDB
Class
DNA binding protein-DNA
Method
X-ray (2.67 Å)
Summary
Crystal structure of the heterotypic nucleosome containing human cenp-a and h3.3
Reference
Arimura Y, Shirayama K, Horikoshi N, Fujita R, Taguchi H, Kagawa W, Fukagawa T, Almouzni G, Kurumizaka H (2014): "Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3." Sci Rep, 4, 7115. doi: 10.1038/srep07115.
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.

Cartoon-block schematics in six views (download the tarball)

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