2F5S

Catalytically inactive (E3Q) MutM crosslinked to oxoG:C containing DNA CC1

2F5S の概要

• エントリーDOI: 10.2210/pdb2f5s/pdb
• 関連するPDBエントリー: 1L1T 1R2Y 2F5N 2F5O 2F5P 2F5Q
• 分子名称: 5'-D(*AP*GP*GP*TP*AP*GP*AP*CP*TP*CP*GP*GP*AP*CP*GP*C)-3', 5'-D(*TP*GP*C*GP*TP*CP*CP*(8OG)P*AP*GP*TP*CP*TP*AP*CP*C)-3', formamidopyrimidine-DNA glycosidase, ... (5 entities in total)
• 機能のキーワード: disulfide crosslink, dna glycosylase, dna repair, damage search, control complex, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Geobacillus stearothermophilus; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 40593.30

構造登録者

Banerjee, A.,Santos, W.L.,Verdine, G.L. (登録日: 2005-11-26, 公開日: 2006-03-07, 最終更新日: 2023-08-23)

主引用文献

Banerjee, A.,Santos, W.L.,Verdine, G.L.
Structure of a DNA glycosylase searching for lesions.
Science, 311:1153-1157, 2006

PubMed Abstract: DNA glycosylases must interrogate millions of base pairs of undamaged DNA in order to locate and then excise one damaged nucleobase. The nature of this search process remains poorly understood. Here we report the use of disulfide cross-linking (DXL) technology to obtain structures of a bacterial DNA glycosylase, MutM, interrogating undamaged DNA. These structures, solved to 2.0 angstrom resolution, reveal the nature of the search process: The protein inserts a probe residue into the helical stack and severely buckles the target base pair, which remains intrahelical. MutM therefore actively interrogates the intact DNA helix while searching for damage.

PubMed: 16497933
DOI: 10.1126/science.1120288

実験手法

X-RAY DIFFRACTION (2.35 Å)