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@ARTICLE{Lecher:23152,
      author       = {Lecher, J. and Schwarz, C.K.W. and Stoldt, M. and Smits,
                      S.H.J. and Willbold, D. and Schmitt, L.},
      title        = {{A}n {RTX} toxin transporters tether ist substrate prior to
                      secretion via the unique function of ist {N}- terminal
                      domain},
      journal      = {Structure},
      volume       = {20},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PreJuSER-23152},
      pages        = {1778 - 1787},
      year         = {2012},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Type 1 secretion systems (T1SS) catalyze the one step
                      protein transport across the membranes of Gram-negative
                      bacteria and are composed of an outer membrane protein, a
                      membrane fusion protein and an ABC transporter. The ABC
                      transporter consists of the canonical nucleotide binding and
                      transmembrane domains. For the toxin hemolysin A (HlyA), the
                      ABC transporter HlyB carries an additional, N-terminal
                      domain sharing about $40\%$ homology to C39 peptidases, but
                      this "C39-like domain" (CLD) is suggested to feature
                      another, yet unknown function. Our functional and structural
                      analysis demonstrates that the CLD is essential for
                      secretion and that it specifically interacts with the
                      unfolded state of HlyA. We determined the nuclear magnetic
                      resonance structure of the CLD as well as the
                      substrate-binding region within the CLD. This mode of
                      action, represents a mechanism within T1SS and answers the
                      question, how a large and unfolded substrate is protected
                      inside the cells during secretion.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22959622},
      UT           = {WOS:000309787900021},
      doi          = {10.1016/j.str.2012.08.005},
      url          = {https://juser.fz-juelich.de/record/23152},
}