2RVQ
Solution structure of the isolated histone H2A-H2B heterodimer
Summary for 2RVQ
| Entry DOI | 10.2210/pdb2rvq/pdb |
| NMR Information | BMRB: 11609 |
| Descriptor | Histone H2A type 1-B/E, Histone H2B type 1-J (2 entities in total) |
| Functional Keywords | nucleosome, histone, h2a, h2b, dna binding protein, cs-rosetta, nuclear protein-nuclear protein complex, nuclear protein/nuclear protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: P04908 P06899 |
| Total number of polymer chains | 2 |
| Total formula weight | 28523.23 |
| Authors | Moriwaki, Y.,Yamane, T.,Ohtomo, H.,Ikeguchi, M.,Kurita, J.,Sato, M.,Nagadoi, A.,Shimojo, H.,Nishimura, Y. (deposition date: 2016-03-28, release date: 2016-05-25, Last modification date: 2024-05-01) |
| Primary citation | Moriwaki, Y.,Yamane, T.,Ohtomo, H.,Ikeguchi, M.,Kurita, J.,Sato, M.,Nagadoi, A.,Shimojo, H.,Nishimura, Y. Solution structure of the isolated histone H2A-H2B heterodimer Sci Rep, 6:24999-24999, 2016 Cited by PubMed Abstract: During chromatin-regulated processes, the histone H2A-H2B heterodimer functions dynamically in and out of the nucleosome. Although detailed crystal structures of nucleosomes have been established, that of the isolated full-length H2A-H2B heterodimer has remained elusive. Here, we have determined the solution structure of human H2A-H2B by NMR coupled with CS-Rosetta. H2A and H2B each contain a histone fold, comprising four α-helices and two β-strands (α1-β1-α2-β2-α3-αC), together with the long disordered N- and C-terminal H2A tails and the long N-terminal H2B tail. The N-terminal αN helix, C-terminal β3 strand, and 310 helix of H2A observed in the H2A-H2B nucleosome structure are disordered in isolated H2A-H2B. In addition, the H2A α1 and H2B αC helices are not well fixed in the heterodimer, and the H2A and H2B tails are not completely random coils. Comparison of hydrogen-deuterium exchange, fast hydrogen exchange, and {(1)H}-(15)N hetero-nuclear NOE data with the CS-Rosetta structure indicates that there is some conformation in the H2A 310 helical and H2B Lys11 regions, while the repression domain of H2B (residues 27-34) exhibits an extended string-like structure. This first structure of the isolated H2A-H2B heterodimer provides insight into its dynamic functions in chromatin. PubMed: 27181506DOI: 10.1038/srep24999 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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