6PA7
The cryo-EM structure of the human DNMT3A2-DNMT3B3 complex bound to nucleosome.
Summary for 6PA7
| Entry DOI | 10.2210/pdb6pa7/pdb |
| EMDB information | 20281 21689 |
| Descriptor | Histone H3.2, S-ADENOSYL-L-HOMOCYSTEINE, Histone H4, ... (10 entities in total) |
| Functional Keywords | methyltransferase, complex, transferase, transferase-dna complex, transferase/dna |
| Biological source | Xenopus laevis (African clawed frog) More |
| Total number of polymer chains | 14 |
| Total formula weight | 541073.19 |
| Authors | Xu, T.H.,Liu, M.,Zhou, X.E.,Liang, G.,Zhao, G.,Xu, H.E.,Melcher, K.,Jones, P.A. (deposition date: 2019-06-11, release date: 2020-06-17, Last modification date: 2024-03-20) |
| Primary citation | Xu, T.H.,Liu, M.,Zhou, X.E.,Liang, G.,Zhao, G.,Xu, H.E.,Melcher, K.,Jones, P.A. Structure of nucleosome-bound DNA methyltransferases DNMT3A and DNMT3B. Nature, 586:151-155, 2020 Cited by PubMed Abstract: CpG methylation by de novo DNA methyltransferases (DNMTs) 3A and 3B is essential for mammalian development and differentiation and is frequently dysregulated in cancer. These two DNMTs preferentially bind to nucleosomes, yet cannot methylate the DNA wrapped around the nucleosome core, and they favour the methylation of linker DNA at positioned nucleosomes. Here we present the cryo-electron microscopy structure of a ternary complex of catalytically competent DNMT3A2, the catalytically inactive accessory subunit DNMT3B3 and a nucleosome core particle flanked by linker DNA. The catalytic-like domain of the accessory DNMT3B3 binds to the acidic patch of the nucleosome core, which orients the binding of DNMT3A2 to the linker DNA. The steric constraints of this arrangement suggest that nucleosomal DNA must be moved relative to the nucleosome core for de novo methylation to occur. PubMed: 32968275DOI: 10.1038/s41586-020-2747-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.94 Å) |
Structure validation
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