4QLC

Crystal structure of chromatosome at 3.5 angstrom resolution

4QLC の概要

• エントリーDOI: 10.2210/pdb4qlc/pdb
• 分子名称: DNA (167-mer), Histone H3, Histone H4, ... (8 entities in total)
• 機能のキーワード: nucleosome core particle, histone fold, chromosome, chromatin, global histone h5, gh5, ncp167, regulation, segregation, chromatosome, gh1, liker histone h5, linker dna, protein-dna complexes, dna binding protein-dna complex, chromatin binding protein-dna complex, chromatin binding protein/dna
• 由来する生物種: Homo sapiens; 詳細
• 細胞内の位置: Nucleus : P02299 P84040 P84051 P02283 P02259
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 218813.70

構造登録者

Jiang, J.S.,Zhou, B.R.,Xiao, T.S.,Bai, Y.W. (登録日: 2014-06-11, 公開日: 2015-07-22, 最終更新日: 2023-09-20)

主引用文献

Zhou, B.R.,Jiang, J.,Feng, H.,Ghirlando, R.,Xiao, T.S.,Bai, Y.
Structural Mechanisms of Nucleosome Recognition by Linker Histones.
Mol.Cell, 33 Suppl 1:2-3, 2015

PubMed Abstract: Linker histones bind to the nucleosome and regulate the structure of chromatin and gene expression. Despite more than three decades of effort, the structural basis of nucleosome recognition by linker histones remains elusive. Here, we report the crystal structure of the globular domain of chicken linker histone H5 in complex with the nucleosome at 3.5 Å resolution, which is validated using nuclear magnetic resonance spectroscopy. The globular domain sits on the dyad of the nucleosome and interacts with both DNA linkers. Our structure integrates results from mutation analyses and previous cross-linking and fluorescence recovery after photobleach experiments, and it helps resolve the long debate on structural mechanisms of nucleosome recognition by linker histones. The on-dyad binding mode of the H5 globular domain is different from the recently reported off-dyad binding mode of Drosophila linker histone H1. We demonstrate that linker histones with different binding modes could fold chromatin to form distinct higher-order structures.

PubMed: 26212454
DOI: 10.1016/j.molcel.2015.06.025

実験手法

X-RAY DIFFRACTION (3.503 Å)