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PLoS One. 2015 Aug 20;10(8):e0135455. doi: 10.1371/journal.pone.0135455. eCollection 2015.

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

Author information

  • 1National Institute of Chemistry, Hajdrihova 19, Ljubljana, Slovenia.
  • 2Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland.
  • 3Institute for Structural and Medicinal Biochemistry, Center for Medical Biotechnology, University of Duisburg-Essen, Essen, Germany.
  • 4NanoBioMedical Center, Adam Mickiewicz University, Poznań, Poland.
  • 5NanoBioMedical Center, Adam Mickiewicz University, Poznań, Poland; Faculty of Physics, Adam Mickiewicz University, Poznań, Poland.
  • 6Department of Chemistry, University of Cambridge, Cambridge, United Kingdom; Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California, San Francisco, California, United States of America.
  • 7Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California, San Francisco, California, United States of America.
  • 8NanoBioMedical Center, Adam Mickiewicz University, Poznań, Poland; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
  • 9Department of Life Sciences, University of Trieste, Trieste, Italy.

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.

PMID:
26291722
PMCID:
PMC4546402
DOI:
10.1371/journal.pone.0135455
[PubMed - indexed for MEDLINE]
Free PMC Article
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