5GSE
Crystal structure of unusual nucleosome
Summary for 5GSE
| Entry DOI | 10.2210/pdb5gse/pdb |
| Descriptor | Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (6 entities in total) |
| Functional Keywords | histone-fold, dna-binding, nucleus, structural protein-dna complex, structural protein/dna |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Nucleus: P68431 P62805 P04908 P06899 |
| Total number of polymer chains | 16 |
| Total formula weight | 350035.90 |
| Authors | Kato, D.,Osakabe, A.,Arimura, Y.,Park, S.Y.,Kurumizaka, H. (deposition date: 2016-08-16, release date: 2017-05-03, Last modification date: 2023-11-08) |
| Primary citation | Kato, D.,Osakabe, A.,Arimura, Y.,Mizukami, Y.,Horikoshi, N.,Saikusa, K.,Akashi, S.,Nishimura, Y.,Park, S.Y.,Nogami, J.,Maehara, K.,Ohkawa, Y.,Matsumoto, A.,Kono, H.,Inoue, R.,Sugiyama, M.,Kurumizaka, H. Crystal structure of the overlapping dinucleosome composed of hexasome and octasome Science, 356:205-208, 2017 Cited by PubMed Abstract: Nucleosomes are dynamic entities that are repositioned along DNA by chromatin remodeling processes. A nucleosome repositioned by the switch-sucrose nonfermentable (SWI/SNF) remodeler collides with a neighbor and forms the intermediate "overlapping dinucleosome." Here, we report the crystal structure of the overlapping dinucleosome, in which two nucleosomes are associated, at 3.14-angstrom resolution. In the overlapping dinucleosome structure, the unusual "hexasome" nucleosome, composed of the histone hexamer lacking one H2A-H2B dimer from the conventional histone octamer, contacts the canonical "octasome" nucleosome, and they intimately associate. Consequently, about 250 base pairs of DNA are left-handedly wrapped in three turns, without a linker DNA segment between the hexasome and octasome moieties. The overlapping dinucleosome structure may provide important information to understand how nucleosome repositioning occurs during the chromatin remodeling process. PubMed: 28408607DOI: 10.1126/science.aak9867 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.14 Å) |
Structure validation
Download full validation report
