9L8U

Cryo-EM structure of ASFV DNA polymerase in a DNA replication state

Summary for 9L8U

• Entry DOI: 10.2210/pdb9l8u/pdb
• EMDB information: 62891
• Descriptor: DNA polymerase, DNA (5'-D(P*TP*AP*AP*GP*GP*TP*AP*GP*GP*GP*GP*AP*GP*GP*AP*T)-3'), DNA (5'-D(P*AP*TP*CP*CP*TP*CP*CP*CP*CP*TP*A)-3'), ... (5 entities in total)
• Functional Keywords: virus, dna polymerase, asfv, dna binding protein/dna, dna binding protein-dna complex
• Biological source: Asfarviridae; More
• Total number of polymer chains: 3
• Total formula weight: 124406.38

Authors

Hu, Z.,Yan, R. (deposition date: 2024-12-28, release date: 2025-12-31, Last modification date: 2026-01-28)

Primary citation

Hu, Z.,SunKang, Y.,Liu, Z.,Huang, L.,Qi, W.,Yan, R.
Structural basis for DNA replication by the African swine fever virus polymerase.
Iscience, 28:114155-114155, 2025

PubMed Abstract: African swine fever virus (ASFV) devastates swine herds and lacks widely available antivirals. We show that the ASFV DNA polymerase beta (Pol β; gene ) localizes to viral replication factories and is required for viral replication. Cryo-electron microscopy structures of Pol β in apo and double-stranded DNA (dsDNA)-bound states reveal pronounced conformational flexibility that enables transitions between functional states. Binding to dsDNA promotes higher-order oligomerization that is essential for catalytic activity, as demonstrated by structure-guided mutagenesis and biochemical assays. These findings define the structural basis of ASFV genome synthesis, highlight the functional significance of Pol β during viral replication, and provide a framework for polymerase-targeted antiviral discovery.

PubMed: 41438038
DOI: 10.1016/j.isci.2025.114155

Experimental method

ELECTRON MICROSCOPY (2.53 Å)