8HG1
The structure of MPXV polymerase holoenzyme in replicating state
Summary for 8HG1
Entry DOI | 10.2210/pdb8hg1/pdb |
EMDB information | 34731 |
Descriptor | DNA polymerase, E4R, DNA polymerase processivity factor component A20, ... (7 entities in total) |
Functional Keywords | mpxv, polymerase, replication, replication-dna complex, replication/dna |
Biological source | Monkeypox virus (monkeypox) More |
Total number of polymer chains | 5 |
Total formula weight | 214116.73 |
Authors | |
Primary citation | Peng, 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: 36520947DOI: 10.1126/science.ade6360 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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