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@ARTICLE{Pinotsis:141075,
      author       = {Pinotsis, N. and Chatziefthimiou, S. D. and Berkemeier, F.
                      and Beuron, F. and Mavridis, I. M. and Konarev, P. V. and
                      Svergun, D. I. and Morris, E. and Rief, M. and Wilmanns, M.
                      and DESY},
      title        = {{S}uperhelical architecture of the myosin filament-linking
                      protein myomesin with unusual elastic properties},
      journal      = {PLoS biology},
      volume       = {10},
      issn         = {1544-9173},
      address      = {Lawrence, KS},
      publisher    = {PLoS},
      reportid     = {PHPPUBDB-24945},
      pages        = {e1001261},
      year         = {2012},
      abstract     = {Active muscles generate substantial mechanical forces by
                      the contraction/relaxation cycle, and, to maintain an
                      ordered state, they require molecular structures of
                      extraordinary stability. These forces are sensed and
                      buffered by unusually long and elastic filament proteins
                      with highly repetitive domain arrays. Members of the
                      myomesin protein family function as molecular bridges that
                      connect major filament systems in the central M-band of
                      muscle sarcomeres, which is a central locus of passive
                      stress sensing. To unravel the mechanism of molecular
                      elasticity in such filament-connecting proteins, we have
                      determined the overall architecture of the complete
                      C-terminal immunoglobulin domain array of myomesin by X-ray
                      crystallography, electron microscopy, solution X-ray
                      scattering, and atomic force microscopy. Our data reveal a
                      dimeric tail-to-tail filament structure of about 360 Å in
                      length, which is folded into an irregular superhelical coil
                      arrangement of almost identical α-helix/domain modules. The
                      myomesin filament can be stretched to about 2.5-fold its
                      original length by reversible unfolding of these linkers, a
                      mechanism that to our knowledge has not been observed
                      previously. Our data explain how myomesin could act as a
                      highly elastic ribbon to maintain the overall structural
                      organization of the sarcomeric M-band. In general terms, our
                      data demonstrate how repetitive domain modules such as those
                      found in myomesin could generate highly elastic protein
                      structures in highly organized cell systems such as muscle
                      sarcomeres.},
      keywords     = {Crystallography, X-Ray / Elasticity / Microscopy, Atomic
                      Force / Microscopy, Electron, Transmission / Models,
                      Molecular / Muscle Proteins: chemistry / Muscle Proteins:
                      ultrastructure / Protein Structure, Quaternary / Protein
                      Structure, Secondary / Protein Structure, Tertiary /
                      Sarcomeres: chemistry / Scattering, Small Angle / Muscle
                      Proteins (NLM Chemicals) / myomesin (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {500},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline BW6 (POF2-54G13) / DORIS Beamline D1.2
                      (POF2-54G13) / DORIS Beamline K1.2 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-BW6-20130405 /
                      G:(DE-H253)POF2-D1.2-20130405 /
                      G:(DE-H253)POF2-K1.2-20130405},
      experiment   = {EXP:(DE-H253)D-K1.2-20150101 / EXP:(DE-H253)D-D1.2-20150101
                      / EXP:(DE-H253)D-BW6-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22347812},
      pmc          = {pmc:PMC3279516},
      UT           = {WOS:000300951500007},
      doi          = {10.1371/journal.pbio.1001261},
      url          = {https://bib-pubdb1.desy.de/record/141075},
}