6S01
Structure of LEDGF PWWP domain bound H3K36 methylated nucleosome
Summary for 6S01
| Entry DOI | 10.2210/pdb6s01/pdb |
| EMDB information | 10069 |
| Descriptor | Histone H3, Histone H4, Histone H2A, ... (7 entities in total) |
| Functional Keywords | ledgf, pwwp, h3k36me3, nucleosome, transcription |
| Biological source | Xenopus laevis (African clawed frog) More |
| Total number of polymer chains | 11 |
| Total formula weight | 270290.78 |
| Authors | Wang, H.,Farnung, L.,Dienemann, C.,Cramer, P. (deposition date: 2019-06-13, release date: 2019-12-18, Last modification date: 2024-10-16) |
| Primary citation | Wang, H.,Farnung, L.,Dienemann, C.,Cramer, P. Structure of H3K36-methylated nucleosome-PWWP complex reveals multivalent cross-gyre binding. Nat.Struct.Mol.Biol., 27:8-13, 2020 Cited by PubMed Abstract: Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here, we report the cryo-electron microscopy structure of the PWWP reader domain of human transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome at 3.2-Å resolution. The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The observed cross-gyre binding may contribute to nucleosome integrity during transcription. The structure also explains how human PWWP domain-containing proteins are recruited to H3K36-methylated regions of the genome for transcription, histone acetylation and methylation, and for DNA methylation and repair. PubMed: 31819277DOI: 10.1038/s41594-019-0345-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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