2XGP

Yeast DNA polymerase eta in complex with C8-2-acetylaminofluorene containing DNA

2XGP の概要

• エントリーDOI: 10.2210/pdb2xgp/pdb
• 関連するPDBエントリー: 1JIH 2WTF 2XGQ
• 分子名称: DNA POLYMERASE ETA, 5'-D(*GP*TP*GP*GP*AP*TP*GP*AP*G)-3', 5'-D(*CP*8FG*CP*TP*CP*AP*TP*CP*CP*AP*C)-3', ... (5 entities in total)
• 機能のキーワード: transferase-dna complex, translesion dna synthesis, dna-binding, dna damage, transferase/dna
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• 細胞内の位置: Nucleus : Q04049
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 134360.45

構造登録者

Scheider, S.,Lammens, K.,Schorr, S.,Hopfner, K.P.,Carell, T. (登録日: 2010-06-07, 公開日: 2010-11-03, 最終更新日: 2023-12-20)

主引用文献

Schorr, S.,Schneider, S.,Lammens, K.,Hopfner, K.P.,Carell, T.
Mechanism of Replication Blocking and Bypass of Y-Family Polymerase Eta by Bulky Acetylaminofluorene DNA Adducts.
Proc.Natl.Acad.Sci.USA, 107:20720-, 2010

PubMed Abstract: Heterocyclic aromatic amines produce bulky C8 guanine lesions in vivo, which interfere and disrupt DNA and RNA synthesis. These lesions are consequently strong replication blocks. In addition bulky adducts give rise to point and frameshift mutations. The translesion synthesis (TLS) DNA polymerase η is able to bypass slowly C8 bulky adduct lesions such as the widely studied 2-aminofluorene-dG and its acetylated analogue mainly in an error-free manner. Replicative polymerases are in contrast fully blocked by the acetylated lesion. Here, we show that TLS efficiency of Pol η depends critically on the size of the bulky adduct forming the lesion. Based on the crystal structure, we show why the bypass reaction is so difficult and we provide a model for the bypass reaction. In our model, TLS is accomplished without rotation of the lesion into the anti conformation as previously thought.

PubMed: 21076032
DOI: 10.1073/PNAS.1008894107

実験手法

X-RAY DIFFRACTION (2.7 Å)