Fig. 3: Cryo-EM structure of apo-DIM2.
From: Multi-layered heterochromatin interaction as a switch for DIM2-mediated DNA methylation
a, b Cryo-EM density map for apo-DIM2 in two opposite views. c, d Atomic model of apo-DIM2 in two opposite views, with individual domains color coded. The SAH molecule and zinc ion are shown in sphere representation. e Cryo-EM density map for the SAH molecule bound to DIM2. f Structural alignment between HP1-bound DIM2 (gray) and apo-DIM2 (cyan). The NT and TRD segments that undergo a disorder-to-order transition upon HP1 binding are indicated by dotted circles. The SAH molecules and zinc ions are shown in sphere representation. g Close-up view of the NT and TRD, with regions that undergo HP1 binding-induced conformational changes are delimited by residue numbers. h In vitro DNA methylation assay of DIM2, WT or mutant, on a (CTA)12/(TAG)12 DNA duplex, in the presence of HP1 and histone H31-24K9me3 peptide. Data are mean ± s.d. (n = 3 biological replicates). Statistical analysis used two-tailed Student’s t test. ****p < 0.0001. Source data are provided as a Source Data file.
