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@ARTICLE{Boer:316984,
      author       = {Boer, D. Roeland and Ruiz-Masó, José Angel and Rueda,
                      Manuel and Petoukhov, Maxim and Machón, Cristina and
                      Svergun, Dmitri I. and Orozco, Modesto and del Solar, Gloria
                      and Coll, Miquel},
      title        = {{C}onformational plasticity of {R}ep{B}, the replication
                      initiator protein of promiscuous streptococcal plasmid
                      p{MV}158},
      journal      = {Scientific reports},
      volume       = {6},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {PUBDB-2017-00354},
      pages        = {20915},
      year         = {2016},
      abstract     = {DNA replication initiation is a vital and tightly regulated
                      step in all replicons and requires an initiator factor that
                      specifically recognizes the DNA replication origin and
                      starts replication. RepB from the promiscuous streptococcal
                      plasmid pMV158 is a hexameric ring protein evolutionary
                      related to viral initiators. Here we explore the
                      conformational plasticity of the RepB hexamer by i) SAXS,
                      ii) sedimentation experiments, iii) molecular simulations
                      and iv) X-ray crystallography. Combining these techniques,
                      we derive an estimate of the conformational ensemble in
                      solution showing that the C-terminal oligomerisation domains
                      of the protein form a rigid cylindrical scaffold to which
                      the N-terminal DNA-binding/catalytic domains are attached as
                      highly flexible appendages, featuring multiple orientations.
                      In addition, we show that the hinge region connecting both
                      domains plays a pivotal role in the observed plasticity.
                      Sequence comparisons and a literature survey show that this
                      hinge region could exists in other initiators, suggesting
                      that it is a common, crucial structural element for DNA
                      binding and manipulation.},
      cin          = {EMBL},
      ddc          = {000},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      experiment   = {EXP:(DE-H253)DORISIII(machine)-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000370055100001},
      pubmed       = {pmid:26875695},
      doi          = {10.1038/srep20915},
      url          = {https://bib-pubdb1.desy.de/record/316984},
}