Summary information and primary citation
- PDB-id
- 4o9m; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- transferase-DNA
- Method
- X-ray (2.295 Å)
- Summary
- Human DNA polymerase beta complexed with adenylated tetrahydrofuran (abasic site) containing DNA
- Reference
- Caglayan M, Batra VK, Sassa A, Prasad R, Wilson SH (2014): "Role of polymerase beta in complementing aprataxin deficiency during abasic-site base excision repair." Nat.Struct.Mol.Biol., 21, 497-499. doi: 10.1038/nsmb.2818.
- Abstract
- DNA polymerase β (pol β) lyase removal of 5'-deoxyribose phosphate (5'-dRP) from base excision repair (BER) intermediates is critical in mammalian BER involving the abasic site. We found that pol β also removes 5'-adenylated dRP from BER intermediates after abortive ligation. The crystal structure of a human pol β-DNA complex showed the 5'-AMP-dRP group positioned in the lyase active site. Pol β expression rescued methyl methanesulfonate sensitivity in aprataxin (hnt3)- and FEN1 (rad27)-deficient yeast.
