8WPF

Structure of monkeypox virus polymerase complex F8-A22-E4-H5 with exogenous DNA bearing one abasic site

8WPF の概要

• エントリーDOI: 10.2210/pdb8wpf/pdb
• EMDBエントリー: 37715
• 分子名称: DNA polymerase, A22R DNA polymerase processivity factor, E4R Uracil-DNA glycosylase, DNA polymerase processivity factor, ... (8 entities in total)
• 機能のキーワード: viral dna replication, monkeypox virus, polymerase, h5, viral protein
• 由来する生物種: Monkeypox virus; 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 311086.25

構造登録者

Wang, X.,Li, N.,Gao, N. (登録日: 2023-10-10, 公開日: 2023-11-29, 最終更新日: 2023-12-27)

主引用文献

Wang, X.,Ma, L.,Li, N.,Gao, N.
Structural insights into the assembly and mechanism of mpox virus DNA polymerase complex F8-A22-E4-H5.
Mol.Cell, 83:4398-, 2023

PubMed Abstract: The DNA replication of mpox virus is performed by the viral polymerase F8 and also requires other viral factors, including processivity factor A22, uracil DNA glycosylase E4, and phosphoprotein H5. However, the molecular roles of these viral factors remain unclear. Here, we characterize the structures of F8-A22-E4 and F8-A22-E4-H5 complexes in the presence of different primer-template DNA substrates. E4 is located upstream of F8 on the template single-stranded DNA (ssDNA) and is catalytically active, highlighting a functional coupling between DNA base-excision repair and DNA synthesis. Moreover, H5, in the form of tetramer, binds to the double-stranded DNA (dsDNA) region downstream of F8 in a similar position as PCNA (proliferating cell nuclear antigen) does in eukaryotic polymerase complexes. Omission of H5 or disruption of its DNA interaction showed a reduced synthesis of full-length DNA products. These structures provide snapshots for the working cycle of the polymerase and generate insights into the mechanisms of these essential factors in viral DNA replication.

PubMed: 37995690
DOI: 10.1016/j.molcel.2023.10.038

実験手法

ELECTRON MICROSCOPY (3 Å)