2XGQ

Structure of yeast DNA polymerase eta in complex with C8-N-acetyl-2- aminoanthracene containing DNA

Summary for 2XGQ

• Entry DOI: 10.2210/pdb2xgq/pdb
• Related: 1JIH 2WTF 2XGP
• Descriptor: DNA POLYMERASE ETA, 5'-D(*GP*TP*GP*GP*AP*TP*GP*AP*G)-3', 5'-D(*CP*8AG*CP*TP*CP*AP*TP*CP*CP*AP*C)-3', ... (5 entities in total)
• Functional Keywords: transferase-dna complex, translesion dna synthesis, dna-binding, dna damage, transferase/dna
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 6
• Total formula weight: 134348.42

Authors

Schneider, S.,Schorr, S.,Carell, T. (deposition date: 2010-06-07, release date: 2010-11-03, Last modification date: 2023-12-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)