8AAG
H1-bound palindromic nucleosome, state 1
8AAG の概要
| エントリーDOI | 10.2210/pdb8aag/pdb |
| EMDBエントリー | 15143 15144 15146 15147 15156 15168 15169 15170 15171 15172 15173 15232 |
| 分子名称 | DNA/RNA (185-MER), Histone H1.0-B, Histone H3.2, ... (7 entities in total) |
| 機能のキーワード | linker histone h1, nucleosome, gene regulation |
| 由来する生物種 | synthetic construct 詳細 |
| タンパク質・核酸の鎖数 | 11 |
| 化学式量合計 | 252692.33 |
| 構造登録者 | Alegrio Louro, J.,Beinsteiner, B.,Cheng, T.C.,Patel, A.K.M.,Boopathi, R.,Angelov, D.,Hamiche, A.,Bednar, J.,Kale, S.,Dimitrov, S.,Klaholz, B. (登録日: 2022-07-01, 公開日: 2022-12-14, 最終更新日: 2024-07-24) |
| 主引用文献 | Louro, J.A.,Boopathi, R.,Beinsteiner, B.,Mohideen Patel, A.K.,Cheng, T.C.,Angelov, D.,Hamiche, A.,Bendar, J.,Kale, S.,Klaholz, B.P.,Dimitrov, S. Nucleosome dyad determines the H1 C-terminus collapse on distinct DNA arms. Structure, 31:201-, 2023 Cited by PubMed Abstract: Nucleosomes are symmetric structures. However, binding of linker histones generates an inherently asymmetric H1-nucleosome complex, and whether this asymmetry is transmitted to the overall nucleosome structure, and therefore also to chromatin, is unclear. Efforts to investigate potential asymmetry due to H1s have been hampered by the DNA sequence, which naturally differs in each gyre. To overcome this issue, we designed and analyzed by cryo-EM a nucleosome reconstituted with a palindromic (601L) 197-bp DNA. As in the non-palindromic 601 sequence, H1 restricts linker DNA flexibility but reveals partial asymmetrical unwrapping. However, in contrast to the non-palindromic nucleosome, in the palindromic nucleosome H1 CTD collapses to the proximal linker. Molecular dynamics simulations show that this could be dictated by a slightly tilted orientation of the globular domain (GD) of H1, which could be linked to the DNA sequence of the nucleosome dyad. PubMed: 36610392DOI: 10.1016/j.str.2022.12.005 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (10 Å) |
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