1TVA

HUMAN DNA POLYMERASE BETA COMPLEXED WITH NICKED DNA CONTAINING A MISMATCHED TEMPLATE THYMIDINE AND INCOMING CYTIDINE

1TVA の概要

• エントリーDOI: 10.2210/pdb1tva/pdb
• 関連するPDBエントリー: 1BPZ 1TV9
• 分子名称: 5'-D(*CP*CP*GP*AP*CP*TP*GP*CP*GP*CP*AP*TP*CP*AP*GP*C)-3', 5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*CP*C)-3', 5'-D(P*GP*TP*CP*GP*G)-3', ... (8 entities in total)
• 機能のキーワード: nucleotidyltransferase, dna repair, dna mismatch, base excision repair, transferase-dna complex, transferase/dna
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P06746
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 48161.60

構造登録者

Krahn, J.M.,Beard, W.A.,Wilson, S.H. (登録日: 2004-06-29, 公開日: 2004-11-23, 最終更新日: 2024-02-14)

主引用文献

Krahn, J.M.,Beard, W.A.,Wilson, S.H.
Structural insights into DNA polymerase Beta deterrents for misincorporation support an induced-fit mechanism for fidelity
Structure, 12:1823-1832, 2004

PubMed Abstract: DNA polymerases generally select the correct nucleotide from a pool of structurally similar molecules to preserve Watson-Crick base-pairing rules. We report the structure of DNA polymerase beta with DNA mismatches situated in the polymerase active site. This was achieved by using nicked product DNA that traps the mispair (template-primer, A-C or T-C) in the nascent base pair binding pocket. The structure of each mispair complex indicates that the bases do not form hydrogen bonds with one another, but form a staggered arrangement where the bases of the mispair partially overlap. This prevents closure/opening of the N subdomain that is believed to be required for catalytic cycling. The partially open conformation of the N subdomain results in distinct hydrogen bonding networks that are unique for each mispair. These structures define diverse molecular aspects of misinsertion that are consistent with the induced-fit model for substrate specificity.

PubMed: 15458631
DOI: 10.1016/j.str.2004.08.001

実験手法

X-RAY DIFFRACTION (2.6 Å)