7K5Y
Cryo-EM structure of a chromatosome containing human linker histone H1.4
Summary for 7K5Y
| Entry DOI | 10.2210/pdb7k5y/pdb |
| Related | 7K5X |
| EMDB information | 22684 |
| Descriptor | Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (8 entities in total) |
| Functional Keywords | chromatosome, nucleosome, linker histones, single-chain antibody, charge-charge interaction, chromatin, nuclear protein, nuclear protein-dna complex, nuclear protein/dna |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 13 |
| Total formula weight | 312139.49 |
| Authors | Zhou, B.-R.,Bai, Y. (deposition date: 2020-09-17, release date: 2020-11-25, Last modification date: 2024-03-06) |
| Primary citation | Zhou, B.R.,Feng, H.,Kale, S.,Fox, T.,Khant, H.,de Val, N.,Ghirlando, R.,Panchenko, A.R.,Bai, Y. Distinct Structures and Dynamics of Chromatosomes with Different Human Linker Histone Isoforms. Mol.Cell, 81:166-182.e6, 2021 Cited by PubMed Abstract: The repeating structural unit of metazoan chromatin is the chromatosome, a nucleosome bound to a linker histone, H1. There are 11 human H1 isoforms with diverse cellular functions, but how they interact with the nucleosome remains elusive. Here, we determined the cryoelectron microscopy (cryo-EM) structures of chromatosomes containing 197 bp DNA and three different human H1 isoforms, respectively. The globular domains of all three H1 isoforms bound to the nucleosome dyad. However, the flanking/linker DNAs displayed substantial distinct dynamic conformations. Nuclear magnetic resonance (NMR) and H1 tail-swapping cryo-EM experiments revealed that the C-terminal tails of the H1 isoforms mainly controlled the flanking DNA orientations. We also observed partial ordering of the core histone H2A C-terminal and H3 N-terminal tails in the chromatosomes. Our results provide insights into the structures and dynamics of the chromatosomes and have implications for the structure and function of chromatin. PubMed: 33238161DOI: 10.1016/j.molcel.2020.10.038 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.76 Å) |
Structure validation
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