1RRQ
MutY adenine glycosylase in complex with DNA containing an A:oxoG pair
1RRQ の概要
エントリーDOI | 10.2210/pdb1rrq/pdb |
関連するPDBエントリー | 1RRS 1RRT |
分子名称 | 5'-D(AP*AP*GP*AP*CP*(8OG)P*TP*GP*GP*AP*C)-3', 5'-D(*TP*GP*TP*CP*CP*AP*AP*GP*TP*CP*T)-3', MutY, ... (6 entities in total) |
機能のキーワード | dna repair, dna glycosylase, 8-oxoguanine, protein-dna complex, hydrolase-dna complex, hydrolase/dna |
由来する生物種 | Geobacillus stearothermophilus |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 49237.09 |
構造登録者 | Fromme, J.C.,Banerjee, A.,Huang, S.J.,Verdine, G.L. (登録日: 2003-12-08, 公開日: 2004-02-17, 最終更新日: 2024-02-14) |
主引用文献 | Fromme, J.C.,Banerjee, A.,Huang, S.J.,Verdine, G.L. Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase Nature, 427:652-656, 2004 Cited by PubMed Abstract: The genomes of aerobic organisms suffer chronic oxidation of guanine to the genotoxic product 8-oxoguanine (oxoG). Replicative DNA polymerases misread oxoG residues and insert adenine instead of cytosine opposite the oxidized base. Both bases in the resulting A*oxoG mispair are mutagenic lesions, and both must undergo base-specific replacement to restore the original C*G pair. Doing so represents a formidable challenge to the DNA repair machinery, because adenine makes up roughly 25% of the bases in most genomes. The evolutionarily conserved enzyme adenine DNA glycosylase (called MutY in bacteria and hMYH in humans) initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. A central issue concerning MutY function is the mechanism by which A*oxoG mispairs are targeted among the vast excess of A*T pairs. Here we report the use of disulphide crosslinking to obtain high-resolution crystal structures of MutY-DNA lesion-recognition complexes. These structures reveal the basis for recognizing both lesions in the A*oxoG pair and for catalysing removal of the adenine base. PubMed: 14961129DOI: 10.1038/nature02306 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.22 Å) |
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