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9V4P

Cryo-EM structure of A. thaliana MET1(610-1534) bound covalently to a hemi-mCpG DNA

Summary for 9V4P
Entry DOI10.2210/pdb9v4p/pdb
EMDB information64782
DescriptorDNA (5'-D(*TP*AP*A*TP*GP*AP*CP*AP*TP*AP*(5CM)P*GP*AP*TP*CP*CP*AP*AP*TP*C)-3'), DNA (5'-D(*GP*AP*TP*TP*GP*GP*AP*TP*(C49)P*GP*TP*AP*TP*GP*TP*CP*AP*TP*TP*A)-3'), DNA (cytosine-5)-methyltransferase 1, ... (6 entities in total)
Functional Keywordsdna methylation, met1, cryo-em structure, epigenetic regulation, gene regulation/dna, gene regulation-dna complex
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains3
Total formula weight116466.55
Authors
Zhang, Z.,Li, W.,Liu, Y.,Du, J. (deposition date: 2025-05-24, release date: 2025-11-26)
Primary citationZhang, Z.,Li, W.,Liu, Y.,Chi, C.,Nan, J.,Wang, C.,Zhu, Y.,Zhao, J.,Xue, Y.,Li, Y.,Wang, P.,Zhai, J.,Du, J.
Structural insights into plant DNA CG methylation maintenance by MET1.
Plant Cell, 37:-, 2025
Cited by
PubMed Abstract: DNA methylation plays critical roles in eukaryotic gene silencing, genome defense, and the suppression of transposable elements. During DNA replication, DNA methylation is diluted and must therefore be restored through maintenance DNA methylation. In plants, in addition to symmetric CG methylation, non-CG methylation is also abundant, with the maintenance of each DNA methylation pattern employing different pathways. Here, we investigate the molecular basis of CG maintenance methylation by plant METHYLTRANSFERASE 1 (MET1), an ortholog of mammalian DNA Methyltransferase 1 (DNMT1). The cryogenic electron microscopy structure of full-length Arabidopsis (Arabidopsis thaliana) MET1 reveals a unique autoinhibitory mechanism that is distinct from that of DNMT1. The structure of the MET1 catalytic domain in complex with hemimethylated substrate DNA suggests specific recognition of hemimethylated CG DNA and reveals the catalytic mechanism. Overall, our study illuminates the molecular basis of MET1 autoinhibition and its preference for hemimethylated DNA substrates.
PubMed: 41082561
DOI: 10.1093/plcell/koaf244
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.34 Å)
Structure validation

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