6NQA
Active state Dot1L bound to the H2B-Ubiquitinated nucleosome, 1-to-1 complex
Summary for 6NQA
| Entry DOI | 10.2210/pdb6nqa/pdb |
| EMDB information | 0468 0480 9384 |
| Descriptor | 601 DNA Strand 1, 601 DNA Strand 2, Histone H4, ... (9 entities in total) |
| Functional Keywords | ubiquitin, nucleosome, methyltransferase, structural protein-transferase-dna complex, structural protein/transferase/dna |
| Biological source | synthetic construct More |
| Total number of polymer chains | 12 |
| Total formula weight | 254982.29 |
| Authors | Worden, E.J.,Hoffmann, N.A.,Wolberger, C. (deposition date: 2019-01-19, release date: 2019-02-20, Last modification date: 2024-10-16) |
| Primary citation | Worden, E.J.,Hoffmann, N.A.,Hicks, C.W.,Wolberger, C. Mechanism of Cross-talk between H2B Ubiquitination and H3 Methylation by Dot1L. Cell, 176:1490-1501.e12, 2019 Cited by PubMed Abstract: Methylation of histone H3 K79 by Dot1L is a hallmark of actively transcribed genes that depends on monoubiquitination of H2B K120 (H2B-Ub) and is an example of histone modification cross-talk that is conserved from yeast to humans. We report here cryo-EM structures of Dot1L bound to ubiquitinated nucleosome that show how H2B-Ub stimulates Dot1L activity and reveal a role for the histone H4 tail in positioning Dot1L. We find that contacts mediated by Dot1L and the H4 tail induce a conformational change in the globular core of histone H3 that reorients K79 from an inaccessible position, thus enabling this side chain to insert into the active site in a position primed for catalysis. Our study provides a comprehensive mechanism of cross-talk between histone ubiquitination and methylation and reveals structural plasticity in histones that makes it possible for histone-modifying enzymes to access residues within the nucleosome core. PubMed: 30765112DOI: 10.1016/j.cell.2019.02.002 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.54 Å) |
Structure validation
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