9mvy

Crystal structure of ZMET2 in complex with unmethylated CTG DNA and a histone H3Kc9me2 peptide

spinqualitylabelsall models 9mvy, resolution 2.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9mvy is a 10 chain structure with sequence from Zea mays and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.71Å Ligands: C49, M2L, SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CMT1_MAIZE Publication Abstract from PubMed DNA methylation is an important epigenetic mechanism that controls the assembly of heterochromatin and gene expression. In plants, DNA methylation occurs in both CG and non-CG contexts, with non-CG methylation showing notable substrate sequence dependence. The plant DNA methyltransferase CMT3 mediates maintenance of CHG (H = A, C, or T) DNA methylation, with a strong substrate preference for the hemimethylated CWG (W = A, T) motif. Yet, the underlying mechanism remains elusive. Here we present a crystal structure of ZMET2, the CMT3 ortholog from Zea mays (maize), in complex with a DNA substrate containing an unmethylated CTG motif and a histone peptide carrying a mimic of the histone H3K9me2 modification. Structural comparison of the ZMET2-CTG complex with the previously reported structure of ZMET2 bound to hemimethylated CAG DNA reveals similar but distinct protein-DNA interactions centered on the CWG motif, providing insight into the methylation state- and substrate sequence-specific ZMET2/CMT3-substrate interaction. Furthermore, our combined structural and biochemical analysis reveals a role for the +3-flanking base of the target cytosine in fine-tuning ZMET2-mediated DNA methylation and its functional interplay with the +1- and +2-flanking sites. Together, these results provide deep mechanistic insights into the substrate specificity of CMT3 DNA methyltransferases in plants. Structure of an Unfavorable de Novo DNA Methylation Complex of Plant Methyltransferase ZMET2.,Herle G, Fang J, Song J J Mol Biol. 2025 May 5;437(17):169186. doi: 10.1016/j.jmb.2025.169186. PMID:40335018 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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