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@ARTICLE{Gustavsson:613884,
      author       = {Gustavsson, Emil and Grünewald, Kay and Elias, Per and
                      Hällberg, B Martin},
      title        = {{D}ynamics of the {H}erpes simplex virus {DNA} polymerase
                      holoenzyme during {DNA} synthesis and proof-reading revealed
                      by {C}ryo-{EM}},
      journal      = {Nucleic acids symposium series},
      volume       = {52},
      number       = {12},
      issn         = {0305-1048},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {PUBDB-2024-05663},
      pages        = {7292-7304},
      year         = {2024},
      note         = {The CryoEM Facility at CSSB is supported by the UHH and DFG
                      [INST 152/772-1|152/774-1|152/775-1|152/776-1|152/777-1
                      FUGG].},
      abstract     = {Herpes simplex virus 1 (HSV-1), a double-stranded DNA
                      virus, replicates using seven essential proteins encoded by
                      its genome. Among these, the UL30 DNA polymerase, complexed
                      with the UL42 processivity factor, orchestrates leading and
                      lagging strand replication of the 152 kb viral genome. UL30
                      polymerase is a prime target for antiviral therapy, and
                      resistance to current drugs can arise in immunocompromised
                      individuals. Using electron cryo-microscopy (cryo-EM), we
                      unveil the dynamic changes of the UL30/UL42 complex with DNA
                      in three distinct states. First, a pre-translocation state
                      with an open fingers domain ready for nucleotide
                      incorporation. Second, a halted elongation state where the
                      fingers close, trapping dATP in the dNTP pocket. Third, a
                      DNA-editing state involving significant conformational
                      changes to allow DNA realignment for exonuclease activity.
                      Additionally, the flexible UL30 C-terminal domain interacts
                      with UL42, forming an extended positively charged surface
                      binding to DNA, thereby enhancing processive synthesis.
                      These findings highlight substantial structural shifts in
                      the polymerase and its DNA interactions during replication,
                      offering insights for future antiviral drug development.},
      cin          = {FS-CS / CSSB-LIV-KG},
      ddc          = {540},
      cid          = {I:(DE-H253)FS-CS-20210408 /
                      I:(DE-H253)CSSB-LIV-KG-20220525},
      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-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38806233},
      UT           = {WOS:001233236800001},
      doi          = {10.1093/nar/gkae374},
      url          = {https://bib-pubdb1.desy.de/record/613884},
}