4DA4

Structure of mouse DNMT1 (731-1602) bound to hemimethylated CpG DNA

4DA4 の概要

• エントリーDOI: 10.2210/pdb4da4/pdb
• 分子名称: DNA (cytosine-5)-methyltransferase 1, DNA_UPPER_STRAND, DNA_LOWER_STRAND, ... (7 entities in total)
• 機能のキーワード: maintenance dna methylation, covalent complex, transferase-dna complex, transferase/dna
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Nucleus: P13864
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 213997.43

構造登録者

Song, J.,Patel, D.J. (登録日: 2012-01-12, 公開日: 2012-02-22, 最終更新日: 2024-02-28)

主引用文献

Song, J.,Teplova, M.,Ishibe-Murakami, S.,Patel, D.J.
Structure-Based Mechanistic Insights into DNMT1-Mediated Maintenance DNA Methylation.
Science, 335:709-712, 2012

PubMed Abstract: DNMT1, the major maintenance DNA methyltransferase in animals, helps to regulate gene expression, genome imprinting, and X-chromosome inactivation. We report on the crystal structure of a productive covalent mouse DNMT1(731-1602)-DNA complex containing a central hemimethylated CpG site. The methyl group of methylcytosine is positioned within a shallow hydrophobic concave surface, whereas the cytosine on the target strand is looped out and covalently anchored within the catalytic pocket. The DNA is distorted at the hemimethylated CpG step, with side chains from catalytic and recognition loops inserting through both grooves to fill an intercalation-type cavity associated with a dual base flip-out on partner strands. Structural and biochemical data establish how a combination of active and autoinhibitory mechanisms ensures the high fidelity of DNMT1-mediated maintenance DNA methylation.

PubMed: 22323818
DOI: 10.1126/science.1214453

実験手法

X-RAY DIFFRACTION (2.6 Å)