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@ARTICLE{Schwarz:16637,
      author       = {Schwarz, C.K.W. and Tschapek, B. and Jumpertz, T. and
                      Jenewein, S. and Lecher, J. and Willbold, D. and Panjikar,
                      S. and Halland, B. and Smits, S.H.J. and Schmitt, L.},
      title        = {{C}rystallisation and preliminary {X}-ray crystallographic
                      studies of an oligomeric species of a refolded {C}39
                      peptidase-like domain of the {E}scherichia coli {ABC}
                      transporter {H}aemolysin {B}},
      journal      = {Acta crystallographica / F},
      volume       = {67},
      issn         = {1744-3091},
      address      = {Oxford [u.a.]},
      publisher    = {Blackwell},
      reportid     = {PreJuSER-16637},
      pages        = {630 - 633},
      year         = {2011},
      note         = {We would like to acknowledge Solvej Siedler for important
                      assistance during the initial stages of this project. This
                      work was funded by the EDICT (European Initiative on
                      Channels and Transporters) consortium FP7 Theme
                      (Health-2007-2.1.1-5) to BT and LS. We thank the Ministry of
                      Innovation, Science and Research of the German Federal State
                      North Rhine-Westphalia (NRW) and the Heinrich Heine
                      University Dusseldorf (scholarship from the CLIB-Graduate
                      Cluster Industrial Biotechnology to CKWS).},
      abstract     = {The ABC transporter haemolysin B (HlyB) from Escherichia
                      coli is part of a type I secretion system that translocates
                      a 110 kDa toxin in one step across both membranes of this
                      Gram-negative bacterium in an ATP-dependent manner. Sequence
                      analysis indicates that HlyB contains a C39 peptidase-like
                      domain at its N-terminus. C39 domains are thiol-dependent
                      peptidases that cleave their substrates after a GG motif.
                      Interestingly, the catalytically invariant cysteine is
                      replaced by a tyrosine in the C39-like domain of HlyB. Here,
                      the overexpression, purification and crystallization of the
                      isolated C39-like domain are described as a first step
                      towards obtaining structural insights into this domain and
                      eventually answering the question concerning the function of
                      a degenerated C39 domain in the ABC transporter HlyB.},
      keywords     = {ATP-Binding Cassette Transporters: chemistry / Bacterial
                      Proteins: chemistry / Carrier Proteins: chemistry /
                      Crystallization / Crystallography, X-Ray / Escherichia coli:
                      chemistry / Hemolysin Proteins: chemistry / Protein
                      Multimerization / Protein Refolding / ATP-Binding Cassette
                      Transporters (NLM Chemicals) / Bacterial Proteins (NLM
                      Chemicals) / Carrier Proteins (NLM Chemicals) / Hemolysin
                      Proteins (NLM Chemicals) / Hlyb protein, Bacteria (NLM
                      Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {530},
      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    = {Biochemical Research Methods / Biochemistry $\&$ Molecular
                      Biology / Biophysics / Crystallography},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21543878},
      pmc          = {pmc:PMC3087657},
      UT           = {WOS:000290235900025},
      doi          = {10.1107/S1744309111010876},
      url          = {https://juser.fz-juelich.de/record/16637},
}