3K57

Crystal structure of E.coli Pol II-normal DNA-dATP ternary complex

3K57 の概要

• エントリーDOI: 10.2210/pdb3k57/pdb
• 関連するPDBエントリー: 3K58 3K59 3K5A 3K5L 3K5M 3K5N 3K5O
• 分子名称: DNA polymerase II, DNA (5'-D(*G*TP*AP*TP*GP*TP*AP*CP*GP*CP*TP*AP*GP*GP*CP*AP*CP*G)-3'), DNA (5'-D(*GP*TP*GP*CP*CP*TP*AP*GP*CP*GP*TP*AP*(DOC))-3'), ... (6 entities in total)
• 機能のキーワード: protein-dna complex, dna damage, dna repair, dna-binding, dna-directed dna polymerase, nucleotidyltransferase, sos response, transferase, transferase-dna complex, transferase/dna
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 100507.71

構造登録者

Yang, W.,Wang, F. (登録日: 2009-10-06, 公開日: 2010-02-09, 最終更新日: 2023-09-06)

主引用文献

Wang, F.,Yang, W.
Structural insight into translesion synthesis by DNA Pol II
Cell(Cambridge,Mass.), 139:1279-1289, 2009

PubMed Abstract: E. coli DNA Pol II and eukaryotic Rev3 are B-family polymerases that can extend primers past a damaged or mismatched site when the high-fidelity replicative polymerases in the same family are ineffective. We report here the biochemical and structural properties of DNA Pol II that facilitate this translesion synthesis. DNA Pol II can extend primers past lesions either directly or by template skipping, in which small protein cavities outside of the active site accommodate looped-out template nucleotides 1 or 2 bp upstream. Because of multiple looping-out alternatives, mutation spectra of bypass synthesis are complicated. Moreover, translesion synthesis is enhanced by altered partitioning of DNA substrate between the polymerase active site and the proofreading exonuclease site. Compared to the replicative B family polymerases, DNA Pol II has subtle amino acid changes remote from the active site that allow it to replicate normal DNA with high efficiency yet conduct translesion synthesis when needed.

PubMed: 20064374
DOI: 10.1016/j.cell.2009.11.043

実験手法

X-RAY DIFFRACTION (2.08 Å)