6L4A
H3-H3-H3 tri-nucleosome with the 22 base-pair linker DNA
Summary for 6L4A
Entry DOI | 10.2210/pdb6l4a/pdb |
EMDB information | 0770 |
Descriptor | Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (6 entities in total) |
Functional Keywords | chromatin, nucleosome, centromere, nuclear protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 26 |
Total formula weight | 635984.96 |
Authors | Takizawa, Y.,Ho, C.-H.,Tachiwana, H.,Matsunami, H.,Ohi, M.,Wolf, M.,Kurumizaka, H. (deposition date: 2019-10-16, release date: 2019-12-04, Last modification date: 2024-03-27) |
Primary citation | Takizawa, Y.,Ho, C.H.,Tachiwana, H.,Matsunami, H.,Kobayashi, W.,Suzuki, M.,Arimura, Y.,Hori, T.,Fukagawa, T.,Ohi, M.D.,Wolf, M.,Kurumizaka, H. Cryo-EM Structures of Centromeric Tri-nucleosomes Containing a Central CENP-A Nucleosome. Structure, 28:44-, 2020 Cited by PubMed Abstract: The histone H3 variant CENP-A is a crucial epigenetic marker for centromere specification. CENP-A forms a characteristic nucleosome and dictates the higher-order configuration of centromeric chromatin. However, little is known about how the CENP-A nucleosome affects the architecture of centromeric chromatin. In this study, we reconstituted tri-nucleosomes mimicking a centromeric nucleosome arrangement containing the CENP-A nucleosome, and determined their 3D structures by cryoelectron microscopy. The H3-CENP-A-H3 tri-nucleosomes adopt an untwisted architecture, with an outward-facing linker DNA path between nucleosomes. This is distinct from the H3-H3-H3 tri-nucleosome architecture, with an inward-facing DNA path. Intriguingly, the untwisted architecture may allow the CENP-A nucleosome to be exposed to the solvent in the condensed chromatin model. These results provide a structural basis for understanding the 3D configuration of CENP-A-containing chromatin, and may explain how centromeric proteins can specifically target the CENP-A nucleosomes buried in robust amounts of H3 nucleosomes in centromeres. PubMed: 31711756DOI: 10.1016/j.str.2019.10.016 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (12.3 Å) |
Structure validation
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