4ONJ
Crystal structure of the catalytic domain of ntDRM
4ONJ の概要
| エントリーDOI | 10.2210/pdb4onj/pdb |
| 関連するPDBエントリー | 4ONQ |
| 分子名称 | DNA methyltransferase, SINEFUNGIN (2 entities in total) |
| 機能のキーワード | dna methyltransferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| 由来する生物種 | Nicotiana tabacum (tobacco) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 81779.28 |
| 構造登録者 | |
| 主引用文献 | Zhong, X.,Du, J.,Hale, C.J.,Gallego-Bartolome, J.,Feng, S.,Vashisht, A.A.,Chory, J.,Wohlschlegel, J.A.,Patel, D.J.,Jacobsen, S.E. Molecular Mechanism of Action of Plant DRM De Novo DNA Methyltransferases. Cell(Cambridge,Mass.), 157:1050-1060, 2014 Cited by PubMed Abstract: DNA methylation is a conserved epigenetic gene-regulation mechanism. DOMAINS REARRANGED METHYLTRANSFERASE (DRM) is a key de novo methyltransferase in plants, but how DRM acts mechanistically is poorly understood. Here, we report the crystal structure of the methyltransferase domain of tobacco DRM (NtDRM) and reveal a molecular basis for its rearranged structure. NtDRM forms a functional homodimer critical for catalytic activity. We also show that Arabidopsis DRM2 exists in complex with the small interfering RNA (siRNA) effector ARGONAUTE4 (AGO4) and preferentially methylates one DNA strand, likely the strand acting as the template for RNA polymerase V-mediated noncoding RNA transcripts. This strand-biased DNA methylation is also positively correlated with strand-biased siRNA accumulation. These data suggest a model in which DRM2 is guided to target loci by AGO4-siRNA and involves base-pairing of associated siRNAs with nascent RNA transcripts. PubMed: 24855943DOI: 10.1016/j.cell.2014.03.056 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.807 Å) |
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