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8AAG

H1-bound palindromic nucleosome, state 1

8AAG の概要
エントリーDOI10.2210/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
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: 36610392
DOI: 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)
構造検証レポート
Validation report summary of 8aag
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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