9ZGF
The complex of HSV-1 proteins UL9 and ICP8 with forked DNA
Summary for 9ZGF
| Entry DOI | 10.2210/pdb9zgf/pdb |
| EMDB information | 74190 |
| Descriptor | Major DNA-binding protein, Replication origin-binding protein, DNA (40-MER), ... (7 entities in total) |
| Functional Keywords | dna replication, protein-dna complex, replication-dna complex, replication/dna |
| Biological source | Human alphaherpesvirus 1 strain 17 More |
| Total number of polymer chains | 4 |
| Total formula weight | 245235.24 |
| Authors | Baranovskiy, A.G.,Morstadt, L.M.,Romero, E.E.,Babayeva, N.D.,Tahirov, T.H. (deposition date: 2025-12-02, release date: 2026-06-10, Last modification date: 2026-06-24) |
| Primary citation | Baranovskiy, A.G.,Morstadt, L.M.,Romero, E.E.,Babayeva, N.D.,Tahirov, T.H. Structural insights into HSV-1 origin unwinding by the viral proteins UL9 and ICP8. Nucleic Acids Res., 54:-, 2026 Cited by PubMed Abstract: Herpes simplex virus type 1 (HSV-1) causes lifelong infections in human cells and is associated with a range of diseases. HSV-1 DNA replication requires seven viral proteins, including the major DNA-binding protein ICP8, the origin-binding protein UL9, and proteins that comprise the helicase-primase and DNA polymerase complexes. UL9 functions as a DNA helicase that specifically recognizes and binds to the viral origins of replication, OriS and OriL. Here we report the cryo-EM structure of the UL9/ICP8/DNA/ATPγS complex at an overall resolution of 3.18 Å. This structure revealed that UL9 employs an α-helix to separate the DNA strands and captures the initial step of OriS unwinding, in which the C-terminal domain of UL9 specifically binds to the major groove of a DNA double helix, while the N-terminal helicase domain engages the unwound leading and lagging strands. ICP8 interacts with the extreme C-terminal region of UL9, preventing UL9 dimerization. Simultaneously, it binds and stabilizes the leading-strand DNA adjacent to UL9. Together, these findings provide mechanistic insight into UL9-driven DNA unwinding and the cooperative action of UL9 and ICP8 at HSV-1 replication origins, establishing a structural framework for the rational interpretation of prior biochemical data and for the design of new antiviral drugs. PubMed: 42283126DOI: 10.1093/nar/gkag580 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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