Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Assembly and breakage of head-to-head double hexamer reveals mpox virus E5-catalyzed DNA unwinding initiation.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 5176, Year 2025
Publish date	Jun 4, 2025
Authors	Yingxian Cheng / Pu Han / Qi Peng / Ruili Liu / Hao Liu / Bin Yuan / Yunfei Zhao / Lu Kuai / Jianxun Qi / Kai Miao / Yi Shi / George Fu Gao / Han Wang /
PubMed Abstract	The replicative helicase-catalyzed unwinding of the DNA double helix is the initiation of DNA replication. Helicases and primases are functionally related enzymes that have even been expressed as ...The replicative helicase-catalyzed unwinding of the DNA double helix is the initiation of DNA replication. Helicases and primases are functionally related enzymes that have even been expressed as fusion proteins in some organisms and viruses. However, the mechanism underlying DNA unwinding initiation by these helicase-primase fusion enzymes and the functional association between domains have not been elucidated. Herein, we report the cryo-EM structures of mpox virus E5, the founding member of these helicase-primase enzymes, in various enzymatic stages. Notably, E5 forms a head-to-head double hexamer encircling dsDNA, disrupted by the conformational rearrangement of primase domains upon nucleotide incorporation. Five E5-ssDNA-ATP structures further support an ATP cycle-driven non-classical escort model for E5 translocation. Finally, the helicase domain is found to enhance the primase function as a DNA scaffold. Together, our data shed light on the E5-mediated DNA unwinding model including dsDNA loading, DNA melting, ssDNA translocation, and provide a reasonable interpretation for evolutionary preservation of helicase-primase fusion from a functional perspective.
External links	Nat Commun / PubMed:40467608 / PubMed Central
Methods	EM (single particle)
Resolution	2.88 - 3.33 Å
Structure data	60676 9ily EMDB-60676, PDB-9ily: The Cryo-EM structure of MPXV E5 in the apo state Method: EM (single particle) / Resolution: 3.33 Å 60677 9ilz EMDB-60677, PDB-9ilz: The Cryo-EM structure of MPXV E5 in complex with ssDNA Method: EM (single particle) / Resolution: 2.95 Å 60678 9im0 EMDB-60678, PDB-9im0: The Cryo-EM structure of MPXV E5 in complex with ssDNA focused on primase and Zn binding domain Method: EM (single particle) / Resolution: 2.95 Å 60679 9im1 EMDB-60679, PDB-9im1: The Cryo-EM structure of MPXV E5 in complex with ssDNA in intermediate state 1 Method: EM (single particle) / Resolution: 2.88 Å 60680 9im2 EMDB-60680, PDB-9im2: The Cryo-EM structure of MPXV E5 in complex with ssDNA in intermediate state 3 Method: EM (single particle) / Resolution: 3.12 Å EMDB-60681: The Cryo-EM map of MPXV E5 in complex with ssDNA in intermediate state 2 Method: EM (single particle) / Resolution: 2.95 Å EMDB-60682: The Cryo-EM map of MPXV E5 in complex with ssDNA in intermediate state 4 Method: EM (single particle) / Resolution: 3.08 Å EMDB-60683: The Cryo-EM map of MPXV E5 in complex with ssDNA in intermediate state 5 Method: EM (single particle) / Resolution: 3.13 Å 60684 9im3 EMDB-60684, PDB-9im3: The Cryo-EM structure of MPXV E5 head-to-head double hexamer conformation Method: EM (single particle) / Resolution: 3.31 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry ChemComp-AMP: ADENOSINE MONOPHOSPHATE / AMP*YM
Source	monkeypox virus
Keywords	VIRAL PROTEIN / protein / VIRAL PROTEIN/DNA / complex / VIRAL PROTEIN-DNA complex