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@ARTICLE{Wald:603157,
      author       = {Wald, Jiri and Marlovits, Thomas},
      title        = {{H}olliday junction branch migration driven by {AAA}+
                      {ATP}ase motors},
      journal      = {Current opinion in structural biology},
      volume       = {82},
      issn         = {0959-440X},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2024-00794},
      pages        = {102650},
      year         = {2023},
      note         = {Waiting for fulltext},
      abstract     = {Holliday junctions are key intermediate DNA structures
                      during genetic recombination. One of the first Holliday
                      junction-processing protein complexes to be discovered was
                      the well conserved RuvAB branch migration complex present in
                      bacteria that mediates an ATP-dependent movement of the
                      Holliday junction (branch migration). Although the RuvAB
                      complex served as a paradigm for the processing of the
                      Holliday junction, due to technical limitations the detailed
                      structure and underlying mechanism of the RuvAB branch
                      migration complex has until now remained unclear. Recently,
                      structures of a reconstituted RuvAB complex
                      actively-processing a Holliday junction were resolved using
                      time-resolved cryo-electron microscopy. These structures
                      showed distinct conformational states at different stages of
                      the migration process. These structures made it possible to
                      propose an integrated model for RuvAB Holliday junction
                      branch migration. Furthermore, they revealed unexpected
                      insights into the highly coordinated and regulated
                      mechanisms of the nucleotide cycle powering substrate
                      translocation in the hexameric AAA+ RuvB ATPase. Here, we
                      review these latest advances and describe areas for future
                      research.},
      cin          = {CSSB-UKE-TM},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-UKE-TM-20210520},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37604043},
      UT           = {WOS:001144737700001},
      doi          = {10.1016/j.sbi.2023.102650},
      url          = {https://bib-pubdb1.desy.de/record/603157},
}