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8HG1

The structure of MPXV polymerase holoenzyme in replicating state

Summary for 8HG1
Entry DOI10.2210/pdb8hg1/pdb
EMDB information34731
DescriptorDNA polymerase, E4R, DNA polymerase processivity factor component A20, ... (7 entities in total)
Functional Keywordsmpxv, polymerase, replication, replication-dna complex, replication/dna
Biological sourceMonkeypox virus (monkeypox)
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Total number of polymer chains5
Total formula weight214116.73
Authors
Peng, Q.,Xie, Y.F.,Kuai, L.,Wang, H.,Qi, J.X.,Gao, F.,Shi, Y. (deposition date: 2022-11-13, release date: 2022-12-21, Last modification date: 2024-05-29)
Primary citationPeng, Q.,Xie, Y.,Kuai, L.,Wang, H.,Qi, J.,Gao, G.F.,Shi, Y.
Structure of monkeypox virus DNA polymerase holoenzyme.
Science, 379:100-105, 2023
Cited by
PubMed Abstract: The World Health Organization declared mpox (or monkeypox) a public health emergency of international concern in July 2022, and prophylactic and therapeutic measures are in urgent need. The monkeypox virus (MPXV) has its own DNA polymerase F8, together with the processive cofactors A22 and E4, constituting the polymerase holoenzyme for genome replication. Here, we determined the holoenzyme structure in complex with DNA using cryo-electron microscopy at the global resolution of ~2.8 angstroms. The holoenzyme possesses an architecture that suggests a "forward sliding clamp" processivity mechanism for viral DNA replication. MPXV polymerase has a DNA binding mode similar to that of other B-family DNA polymerases from different species. These findings reveal the mechanism of the MPXV genome replication and may guide the development of anti-poxvirus drugs.
PubMed: 36520947
DOI: 10.1126/science.ade6360
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.8 Å)
Structure validation

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