Summary information and primary citation
- PDB-id
-
8hwa;
DSSR-derived features in text and
JSON formats
- Class
- viral protein
- Method
- cryo-EM (3.7 Å)
- Summary
- D5 atp-adp-apo-ssDNA is1
- Reference
-
Li Y, Zhu J, Guo Y, Yan R (2024): "Structural
insight into the assembly and working mechanism of
helicase-primase D5 from Mpox virus."
Nat.Struct.Mol.Biol., 31,
68-81. doi: 10.1038/s41594-023-01142-0.
- Abstract
- The Mpox pandemic, caused by the Mpox virus (or
monkeypox virus, MPXV), has gained global attention. The D5
protein, a putative helicase-primase found in MPXV, plays a
vital role in viral replication and genome uncoating. Here
we determined multiple cryo-EM structures of full-length
hexameric D5 in diverse states. These states were captured
during ATP hydrolysis while moving along the
single-stranded DNA (ssDNA) track. Through comprehensive
structural analysis combined with the helicase activity
system, we revealed that when the primase domain is
truncated or the interaction between the primase and
helicase domains is disrupted, the double-stranded DNA
(dsDNA) unwinds into ssDNA, suggesting a critical
regulatory role of the primase domain. Two transition
states bound with ssDNA substrate during unwinding reveals
that two ATP molecules were consumed to drive DNA moving
forward two nucleotides. Collectively, our findings shed
light on the molecular mechanism that links ATP hydrolysis
to the DNA unwinding in poxviruses.
