6HMF

D-family DNA polymerase - DP1 subunit (3'-5' proof-reading exonuclease) H451 proof-reading deficient variant

6HMF の概要

• エントリーDOI: 10.2210/pdb6hmf/pdb
• 分子名称: DNA polymerase II small subunit, FE (III) ION, ZINC ION, ... (7 entities in total)
• 機能のキーワード: dna polymerase d pold, replication
• 由来する生物種: Pyrococcus abyssi (strain GE5 / Orsay)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107769.52

構造登録者

Raia, P.,Delarue, M.,Sauguet, L. (登録日: 2018-09-12, 公開日: 2019-01-30, 最終更新日: 2024-01-24)

主引用文献

Raia, P.,Carroni, M.,Henry, E.,Pehau-Arnaudet, G.,Brule, S.,Beguin, P.,Henneke, G.,Lindahl, E.,Delarue, M.,Sauguet, L.
Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases.
PLoS Biol., 17:e3000122-e3000122, 2019

PubMed Abstract: PolD is an archaeal replicative DNA polymerase (DNAP) made of a proofreading exonuclease subunit (DP1) and a larger polymerase catalytic subunit (DP2). Recently, we reported the individual crystal structures of the DP1 and DP2 catalytic cores, thereby revealing that PolD is an atypical DNAP that has all functional properties of a replicative DNAP but with the catalytic core of an RNA polymerase (RNAP). We now report the DNA-bound cryo-electron microscopy (cryo-EM) structure of the heterodimeric DP1-DP2 PolD complex from Pyrococcus abyssi, revealing a unique DNA-binding site. Comparison of PolD and RNAPs extends their structural similarities and brings to light the minimal catalytic core shared by all cellular transcriptases. Finally, elucidating the structure of the PolD DP1-DP2 interface, which is conserved in all eukaryotic replicative DNAPs, clarifies their evolutionary relationships with PolD and sheds light on the domain acquisition and exchange mechanism that occurred during the evolution of the eukaryotic replisome.

PubMed: 30657780
DOI: 10.1371/journal.pbio.3000122

実験手法

X-RAY DIFFRACTION (2.6 Å)