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7L4N

Crystal structure of the DRM2 (C397R)-CCG DNA complex

Summary for 7L4N
Entry DOI10.2210/pdb7l4n/pdb
Related7L4C 7L4F 7L4H 7L4K 7L4M
DescriptorDNA (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 Keywordsdna methyltransferase, complex, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
Biological sourceArabidopsis thaliana (Mouse-ear cress)
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Total number of polymer chains3
Total formula weight52245.35
Authors
Fang, J.,Song, J. (deposition date: 2020-12-19, release date: 2021-08-04, Last modification date: 2024-11-06)
Primary citationFang, 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: 34078593
DOI: 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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