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@ARTICLE{Furtmann:884297,
      author       = {Furtmann, Fabia and Porta, Nicola and Hoang, Dai Tri and
                      Reiners, Jens and Schumacher, Julia and Gottstein, Julia and
                      Gohlke, Holger and Smits, Sander H. J.},
      title        = {{C}haracterization of the nucleotide-binding domain
                      {N}sr{F} from the {B}ce{AB}-type {ABC}-transporter {N}sr{FP}
                      from the human pathogen {S}treptococcus agalactiae},
      journal      = {Scientific reports},
      volume       = {10},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2020-03183},
      pages        = {15208},
      year         = {2020},
      abstract     = {Treatment of bacterial infections is a great challenge of
                      our era due to the various resistance mechanisms against
                      antibiotics. Antimicrobial peptides are considered to be
                      potential novel compound as antibiotic treatment. However,
                      some bacteria, especially many human pathogens, are
                      inherently resistant to these compounds, due to the
                      expression of BceAB-type ABC transporters. This rather new
                      transporter family is not very well studied. Here, we report
                      the first full characterization of the nucleotide binding
                      domain of a BceAB type transporter from Streptococcus
                      agalactiae, namely SaNsrF of the transporter SaNsrFP, which
                      confers resistance against nisin and gallidermin. We
                      determined the NTP hydrolysis kinetics and used molecular
                      modeling and simulations in combination with small angle
                      X-ray scattering to obtain structural models of the SaNsrF
                      monomer and dimer. The fact that the SaNsrFH202A variant
                      displayed no ATPase activity was rationalized in terms of
                      changes of the structural dynamics of the dimeric interface.
                      Kinetic data show a clear preference for ATP as a substrate,
                      and the prediction of binding modes allowed us to explain
                      this selectivity over other NTPs.},
      cin          = {JSC / NIC / IBI-7},
      ddc          = {600},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)IBI-7-20200312},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511) / Forschergruppe Gohlke $(hkf7_20170501)$},
      pid          = {G:(DE-HGF)POF3-511 / $G:(DE-Juel1)hkf7_20170501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32938989},
      UT           = {WOS:000573768800016},
      doi          = {10.1038/s41598-020-72237-7},
      url          = {https://juser.fz-juelich.de/record/884297},
}