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@ARTICLE{Lecher:16636,
      author       = {Lecher, J. and Stoldt, M. and Schwarz, C.K.W. and Smits,
                      S.H.J. and Schmitt, L. and Willbold, D.},
      title        = {1{H}, 15{N} and 13³{C} resonance assignment of the
                      {N}-terminal {C}39 peptidase-like domain of the {ABC}
                      transporter {H}aemolysin {B} ({H}ly{B})},
      journal      = {Biomolecular NMR assignments},
      volume       = {5},
      issn         = {1874-2718},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Netherlands},
      reportid     = {PreJuSER-16636},
      pages        = {199 - 201},
      year         = {2011},
      note         = {We would like to thank Melanie Schwarten for helpful
                      discussions. The research has been funded by a fellowship
                      from the International Helmholtz Research School on
                      Biophysics and Soft Matter ("Biosoft") to Justin Lecher. We
                      thank the Ministry of Innovation, Science, and Research of
                      the German Federal State North Rhine-Westphalia (NRW) and
                      the Heinrich-Heine-Universitaet Duesseldorf (scholarship
                      from the CLIB-Graduate Cluster Industrial Biotechnology for
                      Christian Schwarz).},
      abstract     = {ATP-binding cassette (ABC) transporters are ubiquitous
                      integral membrane proteins, which catalyze the translocation
                      of molecules across biological membranes in an ATP-dependent
                      manner. Despite the diversity in the transported substrates,
                      they all share the same architecture, comprised of two
                      transmembrane (TMD) and two nucleotide-binding domains
                      (NBD). Members of the bacteriocin ABC transporter subfamily
                      feature a special domain, belonging to the C39 (cystein
                      protease family 39) peptidase protein family. These domains
                      are assumed to cleave a C-terminal signal sequence from the
                      protein or peptide substrate before or during the transport
                      process. Although the C39 peptidase-like domain of the ABC
                      transporter haemolysin B from E. coli shows no proteolytic
                      activity, it is essential for the function of this
                      transporter. In order to elucidate the contribution of the
                      isolated C39 peptidase-like domain in the whole transport
                      process, the backbone and side chain (1)H, (15)N and
                      (13)C-NMR chemical shifts have been assigned.},
      keywords     = {ATP-Binding Cassette Transporters: chemistry / Catalytic
                      Domain / Escherichia coli: enzymology / Escherichia coli
                      Proteins: chemistry / Hemolysin Proteins: chemistry /
                      Isotopes: chemistry / Nuclear Magnetic Resonance,
                      Biomolecular / ATP-Binding Cassette Transporters (NLM
                      Chemicals) / Escherichia coli Proteins (NLM Chemicals) /
                      Hemolysin Proteins (NLM Chemicals) / Isotopes (NLM
                      Chemicals) / hemolysin B (NLM Chemicals) / J (WoSType)},
      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},
      shelfmark    = {Biophysics / Spectroscopy},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21347827},
      UT           = {WOS:000294559700017},
      doi          = {10.1007/s12104-011-9299-0},
      url          = {https://juser.fz-juelich.de/record/16636},
}