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Structural Model of the Bilitranslocase Transmembrane Domain Supported by NMR and FRET Data

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  • Amrita Roy Choudhury
  • Emilia Sikorska
  • Johannes van den Boom
  • Peter Bayer
  • Łukasz Popenda
  • Kosma Szutkowski
  • Stefan Jurga
  • Massimiliano Bonomi
  • Andrej Sali
  • Igor Zhukov
  • Sabina Passamonti
  • Marjana Novič

Abstract

We present a 3D model of the four transmembrane (TM) helical regions of bilitranslocase (BTL), a structurally uncharacterized protein that transports organic anions across the cell membrane. The model was computed by considering helix-helix interactions as primary constraints, using Monte Carlo simulations. The interactions between the TM2 and TM3 segments have been confirmed by Förster resonance energy transfer (FRET) spectroscopy and nuclear magnetic resonance (NMR) spectroscopy, increasing our confidence in the model. Several insights into the BTL transport mechanism were obtained by analyzing the model. For example, the observed cis-trans Leu-Pro peptide bond isomerization in the TM3 fragment may indicate a key conformational change during anion transport by BTL. Our structural model of BTL may facilitate further studies, including drug discovery.

Suggested Citation

  • Amrita Roy Choudhury & Emilia Sikorska & Johannes van den Boom & Peter Bayer & Łukasz Popenda & Kosma Szutkowski & Stefan Jurga & Massimiliano Bonomi & Andrej Sali & Igor Zhukov & Sabina Passamonti & , 2015. "Structural Model of the Bilitranslocase Transmembrane Domain Supported by NMR and FRET Data," PLOS ONE, Public Library of Science, vol. 10(8), pages 1-16, August.
    • Handle: RePEc:plo:pone00:0135455
    DOI: 10.1371/journal.pone.0135455
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    1. Andrej Perdih & Amrita Roy Choudhury & Špela Župerl & Emilia Sikorska & Igor Zhukov & Tom Solmajer & Marjana Novič, 2012. "Structural Analysis of a Peptide Fragment of Transmembrane Transporter Protein Bilitranslocase," PLOS ONE, Public Library of Science, vol. 7(6), pages 1-14, June.
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