3PT6

Crystal structure of mouse DNMT1(650-1602) in complex with DNA

3PT6 の概要

• エントリーDOI: 10.2210/pdb3pt6/pdb
• 関連するPDBエントリー: 3PT9 3PTA
• 分子名称: DNA (cytosine-5)-methyltransferase 1, DNA (5'-D(*TP*CP*CP*CP*GP*TP*GP*AP*GP*CP*CP*TP*CP*CP*GP*CP*AP*GP*G)-3'), DNA (5'-D(*CP*CP*TP*GP*CP*GP*GP*AP*GP*GP*CP*TP*CP*AP*CP*GP*GP*GP*A)-3'), ... (6 entities in total)
• 機能のキーワード: maintenance dna methylation, transferase-dna complex, transferase/dna
• 由来する生物種: Mus musculus (mouse)
• 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: 240681.47

構造登録者

Song, J.,Patel, D.J. (登録日: 2010-12-02, 公開日: 2010-12-29, 最終更新日: 2024-02-21)

主引用文献

Song, J.,Rechkoblit, O.,Bestor, T.H.,Patel, D.J.
Structure of DNMT1-DNA complex reveals a role for autoinhibition in maintenance DNA methylation.
Science, 331:1036-1040, 2011

PubMed Abstract: Maintenance of genomic methylation patterns is mediated primarily by DNA methyltransferase-1 (DNMT1). We have solved structures of mouse and human DNMT1 composed of CXXC, tandem bromo-adjacent homology (BAH1/2), and methyltransferase domains bound to DNA-containing unmethylated CpG sites. The CXXC specifically binds to unmethylated CpG dinucleotide and positions the CXXC-BAH1 linker between the DNA and the active site of DNMT1, preventing de novo methylation. In addition, a loop projecting from BAH2 interacts with the target recognition domain (TRD) of the methyltransferase, stabilizing the TRD in a retracted position and preventing it from inserting into the DNA major groove. Our studies identify an autoinhibitory mechanism, in which unmethylated CpG dinucleotides are occluded from the active site to ensure that only hemimethylated CpG dinucleotides undergo methylation.

PubMed: 21163962
DOI: 10.1126/science.1195380

実験手法

X-RAY DIFFRACTION (3 Å)