6KXV
Crystal structure of a nucleosome containing Leishmania histone H3
Summary for 6KXV
| Entry DOI | 10.2210/pdb6kxv/pdb |
| Descriptor | Histone H3, Histone H4, Histone H2A type 1-B/E, ... (5 entities in total) |
| Functional Keywords | chromatin, nucleosome, leishmania, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Leishmania major More |
| Total number of polymer chains | 10 |
| Total formula weight | 200772.95 |
| Authors | Dacher, M.,Taguchi, H.,Kujirai, T.,Kurumizaka, H. (deposition date: 2019-09-13, release date: 2020-07-22, Last modification date: 2023-11-22) |
| Primary citation | Dacher, M.,Tachiwana, H.,Horikoshi, N.,Kujirai, T.,Taguchi, H.,Kimura, H.,Kurumizaka, H. Incorporation and influence of Leishmania histone H3 in chromatin. Nucleic Acids Res., 47:11637-11648, 2019 Cited by PubMed Abstract: Immunopathologies caused by Leishmania cause severe human morbidity and mortality. This protozoan parasite invades and persists inside host cells, resulting in disease development. Leishmania modifies the epigenomic status of the host cells, thus probably averting the host cell defense mechanism. To accomplish this, Leishmania may change the host cell chromatin structure. However, the mechanism by which the parasite changes the host cell chromatin has not been characterized. In the present study, we found that ectopically produced Leishmania histone H3, LmaH3, which mimics the secreted LmaH3 in infected cells, is incorporated into chromatin in human cells. A crystallographic analysis revealed that LmaH3 forms nucleosomes with human histones H2A, H2B and H4. We found that LmaH3 was less stably incorporated into the nucleosome, as compared to human H3.1. Consistently, we observed that LmaH3-H4 association was remarkably weakened. Mutational analyses revealed that the specific LmaH3 Trp35, Gln57 and Met98 residues, which correspond to the H3.1 Tyr41, Arg63 and Phe104 residues, might be responsible for the instability of the LmaH3 nucleosome. Nucleosomes containing LmaH3 resisted the Mg2+-mediated compaction of the chromatin fiber. These distinct physical characteristics of LmaH3 support the possibility that histones secreted by parasites during infection may modulate the host chromatin structure. PubMed: 31722422DOI: 10.1093/nar/gkz1040 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.63 Å) |
Structure validation
Download full validation report
