3G6V

DNA synthesis across an abasic lesion by human DNA polymerase-iota

3G6V の概要

• エントリーDOI: 10.2210/pdb3g6v/pdb
• 関連するPDBエントリー: 2fll 3G6X 3G6Y
• 分子名称: DNA polymerase iota, Primer DNA strand, Template DNA strand, ... (6 entities in total)
• 機能のキーワード: dna polymerase, y-family, lesion bypass, abasic site, ternary complex, dna damage, dna repair, dna replication, dna synthesis, dna-binding, dna-directed dna polymerase, magnesium, metal-binding, mutator protein, nucleotidyltransferase, nucleus, schiff base, transferase, replication-dna complex, replication/dna
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 53194.83

構造登録者

Nair, D.T.,Aggarwal, A.K. (登録日: 2009-02-09, 公開日: 2009-05-12, 最終更新日: 2023-09-06)

主引用文献

Nair, D.T.,Johnson, R.E.,Prakash, L.,Prakash, S.,Aggarwal, A.K.
DNA Synthesis across an Abasic Lesion by Human DNA Polymerase iota
Structure, 17:530-537, 2009

PubMed Abstract: Abasic sites are among the most abundant DNA lesions formed in human cells, and they present a strong block to replication. DNA polymerase iota (Poliota) is one of the few DNA Pols that does not follow the A-rule opposite an abasic site. We present here three structures of human Poliota in complex with DNAs containing an abasic lesion and dGTP, dTTP, or dATP as the incoming nucleotide. The structures reveal a mechanism of translesion synthesis across an abasic lesion that differs from that in other Pols. Both the abasic lesion and the incoming dNTPs are intrahelical and are closely apposed across a constricted active site cleft. The dNTPs partake in distinct networks of hydrogen bonds in the "void" opposite the lesion. These different patterns of hydrogen bonds, as well as stacking interactions, may underlie Poliota's small preference for insertion of dGTP over other nucleotides opposite this common lesion.

PubMed: 19368886
DOI: 10.1016/j.str.2009.02.015

実験手法

X-RAY DIFFRACTION (2.2 Å)