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@ARTICLE{Reinke:617263,
      author       = {Reinke, Patrick Y. A. and Heiringhoff, Robin S. and Reindl,
                      Theresia and Baker, Karen and Taft, Manuel H. and Meents,
                      Alke and Mulvihill, Daniel P. and Davies, Owen R. and
                      Fedorov, Roman and Zahn, Michael and Manstein, Dietmar J.},
      title        = {{C}rystal structures of cables formed by the acetylated and
                      unacetylated forms of the {S}chizosaccharomyces pombe
                      tropomyosin orthologue {T}pm{C}dc8},
      journal      = {Biologist},
      volume       = {300},
      number       = {12},
      issn         = {0021-9258},
      address      = {Bethesda, MD},
      publisher    = {American Soc. for Biochemistry and Molecular Biology},
      reportid     = {PUBDB-2024-06660},
      pages        = {107925},
      year         = {2024},
      note         = {ISSN 0021-9258 not unique: **2 hits**. erman Research
                      Foundation (DFG), Grant FE1510/2-1, and the Cluster of
                      Excellence RESIST (Resolving InfectionSusceptibility; EXC
                      2155), project ID: 39087428},
      abstract     = {Cables formed by head-to-tail polymerization of
                      tropomyosin, localized along the length of sarcomeric and
                      cytoskeletal actin filaments, play a key role in regulating
                      a wide range of motile and contractile processes. The
                      stability of tropomyosin cables, their interaction with
                      actin filaments and the functional properties of the
                      resulting co-filaments are thought to be affected by
                      N-terminal acetylation of tropomyosin. Here, we present
                      high-resolution structures of cables formed by acetylated
                      and unacetylated Schizosaccharomyces pombe tropomyosin
                      orthologue TpmCdc8. The crystal structures represent
                      different types of cables, each consisting of TpmCdc8
                      homodimers in a different conformation. The structures show
                      how the interactions of the residues in the overlap junction
                      contribute to cable formation and how local structural
                      perturbations affect the conformational dynamics of the
                      protein and its ability to transmit allosteric signals. In
                      particular, N-terminal acetylation increases the helicity of
                      the adjacent region, which leads to a local reduction in
                      conformational dynamics and consequently to less fraying of
                      the N-terminal region. This creates a more consistent
                      complementary surface facilitating the formation of specific
                      interactions across the overlap junction.},
      cin          = {FS-CFEL-1-BMX / FS-CFEL-1},
      ddc          = {610},
      cid          = {I:(DE-H253)FS-CFEL-1-BMX-20210408 /
                      I:(DE-H253)FS-CFEL-1-20120731},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)
                      / DFG project G:(GEPRIS)390874280 - EXC 2155: RESIST -
                      Resolving Infection Susceptibility (390874280)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3 /
                      G:(GEPRIS)390874280},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39461476},
      UT           = {WOS:001366933400001},
      doi          = {10.1016/j.jbc.2024.107925},
      url          = {https://bib-pubdb1.desy.de/record/617263},
}