3SAV

MUTM Slanted complex 8

3SAV の概要

• エントリーDOI: 10.2210/pdb3sav/pdb
• 関連するPDBエントリー: 3SAR 3SAS 3SAT 3SAU 3SAW 3SBJ
• 分子名称: DNA GLYCOSYLASE, DNA (5'-D(*AP*GP*GP*TP*AP*GP*AP*CP*AP*AP*GP*GP*AP*CP*GP*C)-3'), DNA (5'-D(*TP*GP*CP*GP*T*CP*CP*TP*TP*GP*TP*(CX2)P*TP*AP*CP*C)-3'), ... (5 entities in total)
• 機能のキーワード: dna glycosylase, dna repair, damage search, translocation, disulfide crosslinking, dna damage, dna-binding, glycosidase, hydrolase, lyase, metal-binding, multifunctional enzyme, zinc-finger, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Geobacillus stearothermophilus (Bacillus stearothermophilus); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 40505.24

構造登録者

Spong, M.C.,Qi, Y.,Verdine, G.L. (登録日: 2011-06-03, 公開日: 2012-01-11, 最終更新日: 2023-09-13)

主引用文献

Qi, Y.,Nam, K.,Spong, M.C.,Banerjee, A.,Sung, R.J.,Zhang, M.,Karplus, M.,Verdine, G.L.
Strandwise translocation of a DNA glycosylase on undamaged DNA.
Proc.Natl.Acad.Sci.USA, 109:1086-1091, 2012

PubMed Abstract: Base excision repair of genotoxic nucleobase lesions in the genome is critically dependent upon the ability of DNA glycosylases to locate rare sites of damage embedded in a vast excess of undamaged DNA, using only thermal energy to fuel the search process. Considerable interest surrounds the question of how DNA glycosylases translocate efficiently along DNA while maintaining their vigilance for target damaged sites. Here, we report the observation of strandwise translocation of 8-oxoguanine DNA glycosylase, MutM, along undamaged DNA. In these complexes, the protein is observed to translocate by one nucleotide on one strand while remaining untranslocated on the complementary strand. We further report that alterations of single base-pairs or a single amino acid substitution (R112A) can induce strandwise translocation. Molecular dynamics simulations confirm that MutM can translocate along DNA in a strandwise fashion. These observations reveal a previously unobserved mode of movement for a DNA-binding protein along the surface of DNA.

PubMed: 22219368
DOI: 10.1073/pnas.1111237108

実験手法

X-RAY DIFFRACTION (2.125 Å)