4QLC

Crystal structure of chromatosome at 3.5 angstrom resolution

Summary for 4QLC

• Entry DOI: 10.2210/pdb4qlc/pdb
• Descriptor: DNA (167-mer), Histone H3, Histone H4, ... (8 entities in total)
• Functional Keywords: 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
• Biological source: Homo sapiens; More
• Cellular location: Nucleus : P02299 P84040 P84051 P02283 P02259
• Total number of polymer chains: 11
• Total formula weight: 218813.70

Authors

Jiang, J.S.,Zhou, B.R.,Xiao, T.S.,Bai, Y.W. (deposition date: 2014-06-11, release date: 2015-07-22, Last modification date: 2023-09-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.503 Å)