Skip to main content
. Author manuscript; available in PMC: 2026 Jun 16.
Published in final edited form as: Mol Cell. 2026 Feb 24;86(5):834–850.e9. doi: 10.1016/j.molcel.2026.01.030

Figure 2: Structure of the DNMT3A2/DNMT3B3 tetramer bound to a di-nucleosome.

Figure 2:

a Domain architecture of DNMT3A and DNMT3B isoforms. Catalytic (CD), catalytic-like (CLD), ADD and PWWP domains are indicated. b-c Cryo-EM map of the complex between the DNMT3A2/3B3 tetramer and the 10-8-10 di-nucleosome filtered to 10Å, displayed at a threshold of 0.0239 and colored as in a. d-e Combined focused maps of each DNMT3A2 and DNMT3B3 tetramer and each nucleosome displayed at a threshold of 0.06. Unresolved density for the PWWP domains due to focused refinement is indicated with shaded regions colored pink. f-g Atomic model of the DNMT3A2/DNMT3B3 tetramer bound to a di-nucleosome. Protein domains are colored as in a-e. The 8bp linker DNA separating the two nucleosomes is colored red. h-i Close up view of the proximal (h) and distal (i) acidic patch contact sites in the nucleosome focused maps. Density for the DNMT3B3 arginine anchor is shown as a semi-transparent surface. j Composite map showing the contact between distal DNMT3B3 and the lower nucleosome. k Close up view of the contact point between the distal DNMT3B3 ADD and the histone core. Basic resides of the DNMT3B3 ADD domain in proximity to acidic residues in H3 and H4 are shown in stick representation. See also Figures S2–S4.