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@ARTICLE{Mesarich:139940,
      author       = {Mesarich, Carl H. and Schmitz, Michael and Tremouilhac,
                      Pierre and McGillivray, Duncan J. and Templeton, Matthew D.
                      and Dingley, Andrew},
      title        = {{S}tructure, dynamics and domain organization of the repeat
                      protein {C}in1 from the apple scab fungus},
      journal      = {Biochimica et biophysica acta / Proteins and proteomics},
      volume       = {1824},
      number       = {10},
      issn         = {1570-9639},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2013-05907},
      pages        = {1118 - 1128},
      year         = {2012},
      abstract     = {Venturia inaequalis is a hemi-biotrophic fungus that causes
                      scab disease of apple. A recently-identified gene from this
                      fungus, cin1 (cellophane-induced 1), is up-regulated over
                      1000-fold in planta and considerably on cellophane
                      membranes, and encodes a cysteine-rich secreted protein of
                      523 residues with eight imperfect tandem repeats of ~60
                      amino acids. The Cin1 sequence has no homology to known
                      proteins and appears to be genus-specific; however, Cin1
                      repeats and other repeat domains may be structurally
                      similar. An NMR-derived structure of the first two repeat
                      domains of Cin1 (Cin1-D1D2) and a low-resolution model of
                      the full-length protein (Cin1-FL) using SAXS data were
                      determined. The structure of Cin1-D1D2 reveals that each
                      domain comprises a core helix-loop-helix (HLH) motif as part
                      of a three-helix bundle, and is stabilized by two
                      intra-domain disulfide bonds. Cin1-D1D2 adopts a unique
                      protein fold as DALI and PDBeFOLD analysis identified no
                      structural homology. A (15)N backbone NMR dynamic analysis
                      of Cin1-D1D2 showed that a short stretch of the inter-domain
                      linker has large amplitude motions that give rise to
                      reciprocal domain-domain mobility. This observation was
                      supported by SAXS data modeling, where the scattering length
                      density envelope remains thick at the domain-domain
                      boundary, indicative of inter-domain dynamics. Cin1-FL SAXS
                      data models a loosely-packed arrangement of domains, rather
                      than the canonical parallel packing of adjacent HLH repeats
                      observed in α-solenoid repeat proteins. Together, these
                      data suggest that the repeat domains of Cin1 display a
                      "beads-on-a-string" organization with inherent inter-domain
                      flexibility that is likely to facilitate interactions with
                      target ligands.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000307918300006},
      pubmed       = {pmid:22771296},
      doi          = {10.1016/j.bbapap.2012.06.015},
      url          = {https://juser.fz-juelich.de/record/139940},
}