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@ARTICLE{Braun:202943,
      author       = {Braun, Tatjana and Orlova, Albina and Valegård, Karin and
                      Lindås, Ann-Christin and Schröder, Gunnar and Egelman,
                      Edward H.},
      title        = {{A}rchaeal actin from a hyperthermophile forms a
                      single-stranded filament},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {112},
      number       = {30},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2015-05066},
      pages        = {9340 - 9345},
      year         = {2015},
      abstract     = {The prokaryotic origins of the actin cytoskeleton have been
                      firmly established, but it has become clear that the
                      bacterial actins form a wide variety of different filaments,
                      different both from each other and from eukaryotic F-actin.
                      We have used electron cryomicroscopy (cryo-EM) to examine
                      the filaments formed by the protein crenactin (a
                      crenarchaeal actin) from Pyrobaculum calidifontis, an
                      organism that grows optimally at 90 °C. Although this
                      protein only has $∼20\%$ sequence identity with eukaryotic
                      actin, phylogenetic analyses have placed it much closer to
                      eukaryotic actin than any of the bacterial homologs. It has
                      been assumed that the crenactin filament is double-stranded,
                      like F-actin, in part because it would be hard to imagine
                      how a single-stranded filament would be stable at such high
                      temperatures. We show that not only is the crenactin
                      filament single-stranded, but that it is remarkably similar
                      to each of the two strands in F-actin. A large insertion in
                      the crenactin sequence would prevent the formation of an
                      F-actin-like double-stranded filament. Further, analysis of
                      two existing crystal structures reveals six different
                      subunit-subunit interfaces that are filament-like, but each
                      is different from the others in terms of significant
                      rotations. This variability in the subunit-subunit
                      interface, seen at atomic resolution in crystals, can
                      explain the large variability in the crenactin filaments
                      observed by cryo-EM and helps to explain the variability in
                      twist that has been observed for eukaryotic actin
                      filaments.},
      cin          = {ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000358656500063},
      pubmed       = {pmid:26124094},
      doi          = {10.1073/pnas.1509069112},
      url          = {https://juser.fz-juelich.de/record/202943},
}