7L4N
Crystal structure of the DRM2 (C397R)-CCG DNA complex
Summary for 7L4N
Entry DOI | 10.2210/pdb7l4n/pdb |
Related | 7L4C 7L4F 7L4H 7L4K 7L4M |
Descriptor | DNA (cytosine-5)-methyltransferase DRM2, DNA (5'-D(*TP*AP*AP*AP*TP*TP*CP*GP*GP*AP*TP*TP*AP*GP*GP*AP*AP*T)-3'), DNA (5'-D(*AP*TP*TP*CP*CP*TP*AP*AP*TP*(C49)P*CP*GP*AP*AP*TP*TP*TP*A)-3'), ... (6 entities in total) |
Functional Keywords | dna methyltransferase, complex, dna binding protein, dna binding protein-dna complex, dna binding protein/dna |
Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
Total number of polymer chains | 3 |
Total formula weight | 52245.35 |
Authors | |
Primary citation | Fang, J.,Leichter, S.M.,Jiang, J.,Biswal, M.,Lu, J.,Zhang, Z.M.,Ren, W.,Zhai, J.,Cui, Q.,Zhong, X.,Song, J. Substrate deformation regulates DRM2-mediated DNA methylation in plants. Sci Adv, 7:-, 2021 Cited by PubMed Abstract: DNA methylation is a major epigenetic mechanism critical for gene expression and genome stability. In plants, domains rearranged methyltransferase 2 (DRM2) preferentially mediates CHH (H = C, T, or A) methylation, a substrate specificity distinct from that of mammalian DNA methyltransferases. However, the underlying mechanism is unknown. Here, we report structure-function characterization of DRM2-mediated methylation. An arginine finger from the catalytic loop intercalates into the nontarget strand of DNA through the minor groove, inducing large DNA deformation that affects the substrate preference of DRM2. The target recognition domain stabilizes the enlarged major groove via shape complementarity rather than base-specific interactions, permitting substrate diversity. The engineered DRM2 C397R mutation introduces base-specific contacts with the +2-flanking guanine, thereby shifting the substrate specificity of DRM2 toward CHG DNA. Together, this study uncovers DNA deformation as a mechanism in regulating the specificity of DRM2 toward diverse CHH substrates and illustrates methylome complexity in plants. PubMed: 34078593DOI: 10.1126/sciadv.abd9224 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.247 Å) |
Structure validation
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