Structural Analysis of a Peptide Fragment of Transmembrane Transporter Protein Bilitranslocase
Open Access
- 20 June 2012
- journal article
- research article
- Published by Public Library of Science (PLoS) in PLOS ONE
- Vol. 7 (6), e38967
- https://doi.org/10.1371/journal.pone.0038967
Abstract
Using a combination of genomic and post-genomic approaches is rapidly altering the number of identified human influx carriers. A transmembrane protein bilitranslocase (TCDB 2.A.65) has long attracted attention because of its function as an organic anion carrier. It has also been identified as a potential membrane transporter for cellular uptake of several drugs and due to its implication in drug uptake, it is extremely important to advance the knowledge about its structure. However, at present, only the primary structure of bilitranslocase is known. In our work, transmembrane subunits of bilitranslocase were predicted by a previously developed chemometrics model and the stability of these polypeptide chains were studied by molecular dynamics (MD) simulation. Furthermore, sodium dodecyl sulfate (SDS) micelles were used as a model of cell membrane and herein we present a high-resolution 3D structure of an 18 amino acid residues long peptide corresponding to the third transmembrane part of bilitranslocase obtained by use of multidimensional NMR spectroscopy. It has been experimentally confirmed that one of the transmembrane segments of bilitranslocase has alpha helical structure with hydrophilic amino acid residues oriented towards one side, thus capable of forming a channel in the membrane.This publication has 50 references indexed in Scilit:
- Recent advances in the application of solution NMR spectroscopy to multi-span integral membrane proteinsProgress in Nuclear Magnetic Resonance Spectroscopy, 2009
- A survey of integral α-helical membrane proteinsJournal of Structural and Functional Genomics, 2009
- TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shiftsJournal of Biomolecular NMR, 2009
- CHARMM: The biomolecular simulation programJournal of Computational Chemistry, 2009
- Uniformly Aligned Full-Length Membrane Proteins in Liquid Crystalline Bilayers for Structural CharacterizationJournal of the American Chemical Society, 2007
- Extending the treatment of backbone energetics in protein force fields: Limitations of gas‐phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulationsJournal of Computational Chemistry, 2004
- All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of ProteinsThe Journal of Physical Chemistry B, 1998
- VMD: Visual molecular dynamicsJournal of Molecular Graphics, 1996
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- 1H, 13C and 15N chemical shift referencing in biomolecular NMRJournal of Biomolecular NMR, 1995