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@ARTICLE{Gustavsson:639657,
      author       = {Gustavsson, Emil and Grünewald, Kay and Elias, Per and
                      Hällberg, B Martin},
      title        = {{T}he herpes simplex origin-binding protein: mechanisms for
                      sequence-specific {DNA} binding and dimerization revealed by
                      {C}ryo-{EM}},
      journal      = {Nucleic acids symposium series},
      volume       = {53},
      number       = {19},
      issn         = {0305-1048},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {PUBDB-2025-04614},
      pages        = {gkaf1029},
      year         = {2025},
      note         = {ISSN 1362-4962 not unique: **2 hits**. DFG grant numbers
                      (INST 152/772-1|152/774-1|152/775-1|152/776-1|152/777-1
                      FUGG)},
      abstract     = {Herpes simplex viruses 1 and 2 (HSV-1,2) present growing
                      treatment challenges due to increasing resistance to
                      antivirals targeting viral DNA polymerase, particularly in
                      immunocompromised individuals. The HSV-1 origin-binding
                      protein (OBP), an essential Superfamily 2 (SF2) DNA helicase
                      encoded by the UL9 gene, is a promising alternative
                      therapeutic target. Here, we present cryo-EM structures of
                      OBP at up to 2.8 Å resolution in multiple conformational
                      states, including complexes with the OriS recognition
                      sequence and the non-hydrolyzable ATP analog ATPγS. The
                      structures reveal an unexpected head-to-tail dimer
                      stabilized by the C-terminal domain, where the conserved
                      RVKNL motif mediates sequence-specific DNA recognition. The
                      C-terminal domain extends into the partner monomer,
                      suggesting a regulatory mechanism involving the
                      single-stranded DNA-binding protein ICP8. We also resolve an
                      OBP monomer bound to a DNA hairpin with a 3′
                      single-stranded tail (mini-OriS*), and at lower resolution,
                      a dimer-dimer assembly of two OBP dimers bound
                      simultaneously to OriS or mini-OriS*. These structures
                      uncover the molecular basis of HSV-1 origin recognition and
                      unwinding, and identify multiple druggable interfaces,
                      laying the groundwork for structure-based antiviral
                      development targeting HSV-1 OBP.},
      cin          = {CSSB-LIV-KG / KI},
      ddc          = {540},
      cid          = {I:(DE-H253)CSSB-LIV-KG-20220525 / I:(DE-H253)KI-20130912},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / DFG project G:(GEPRIS)534044797 -
                      Large Scale Data Facility 3 - Anteil Forschungsgroßgerät
                      (LSDF3-FuGG) (534044797)},
      pid          = {G:(DE-HGF)POF4-633 / G:(GEPRIS)534044797},
      experiment   = {EXP:(DE-H253)cryo-EM-20250101 / EXP:(DE-H253)PP-20250101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:41125242},
      doi          = {10.1093/nar/gkaf1029},
      url          = {https://bib-pubdb1.desy.de/record/639657},
}