2AOR

Crystal structure of MutH-hemimethylated DNA complex

2AOR の概要

• エントリーDOI: 10.2210/pdb2aor/pdb
• 関連するPDBエントリー: 2AOQ
• 分子名称: 5'-D(*CP*AP*GP*GP*(6MA)P*TP*CP*CP*AP*AP*GP*CP*TP*TP*GP*GP*AP*TP*CP*CP*TP*G)-3', DNA mismatch repair protein mutH, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: gatc recognition, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Haemophilus influenzae
• 細胞内の位置: Cytoplasm (By similarity): P44688
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63566.79

構造登録者

Lee, J.Y.,Chang, J.,Joseph, N.,Ghirlando, R.,Rao, D.N.,Yang, W. (登録日: 2005-08-13, 公開日: 2005-10-11, 最終更新日: 2023-08-23)

主引用文献

Lee, J.Y.,Chang, J.,Joseph, N.,Ghirlando, R.,Rao, D.N.,Yang, W.
MutH complexed with hemi- and unmethylated DNAs: coupling base recognition and DNA cleavage.
Mol.Cell, 20:155-166, 2005

PubMed Abstract: MutH initiates mismatch repair by nicking the transiently unmethylated daughter strand 5' to a GATC sequence. Here, we report crystal structures of MutH complexed with hemimethylated and unmethylated GATC substrates. Both structures contain two Ca2+ ions jointly coordinated by a conserved aspartate and the scissile phosphate, as observed in the restriction endonucleases BamHI and BglI. In the hemimethylated complexes, the active site is more compact and DNA cleavage is more efficient. The Lys residue in the conserved DEK motif coordinates the nucleophilic water in conjunction with the phosphate 3' to the scissile bond; the same Lys is also hydrogen bonded with a carbonyl oxygen in the DNA binding module. We propose that this Lys, which is conserved in many restriction endonucleases and is replaced by Glu or Gln in BamHI and BglII, is a sensor for DNA binding and the linchpin that couples base recognition and DNA cleavage.

PubMed: 16209953
DOI: 10.1016/j.molcel.2005.08.019

実験手法

X-RAY DIFFRACTION (2 Å)