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Volume 6, Issue 1


Membrane protein reconstitution in nanodiscs for luminescence spectroscopy studies

Maria E. Zoghbi
  • School of Natural Sciences, University of California, Merced, 4225 N. Hospital Road, Atwater, CA 95301, USA
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Guillermo A. Altenberg
  • Corresponding author
  • Department of Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center, 3601 4th Street, Lubbock, TX 79430-6551, USA
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2017-01-26 | DOI: https://doi.org/10.1515/ntrev-2016-0078


ATP-binding cassette (ABC) exporters transport substrates across biological membranes using ATP hydrolysis by a process that involves switching between inward- and outward-facing conformations. Most of the structural studies of ABC proteins have been performed with proteins in detergent micelles, locked in specific conformations and/or at low temperature. In this article, we present recent data from our laboratories where we studied the prototypical ABC exporter MsbA during ATP hydrolysis, at 37°C, reconstituted in a lipid bilayer. These studies were possible through the use of luminescence resonance energy transfer spectroscopy in MsbA reconstituted in nanodiscs. We found major differences between MsbA in these native-like conditions and in previous studies. These include a separation between the nucleotide-binding domains that was much smaller than previously thought, and a large fraction of molecules with associated nucleotide-binding domains in the nucleotide-free apo state. These studies stress the importance of studying membrane proteins in an environment that approaches physiological conditions.

Keywords: ATP-binding cassette; LRET; luminescence resonance energy transfer; MsbA; multidrug resistance


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About the article

Maria E. Zoghbi

Maria E. Zoghbi is an Assistant Professor in the Department of Natural Sciences at the University of California, Merced, CA, USA. She was born in Venezuela, where she studied biology at the Central University of Venezuela, and received her PhD degree from the Venezuelan Institute for Scientific Research. She joined Roger Craig’s laboratory at University of Massachusetts Medical School in 2001 for her doctoral thesis and first postdoctoral position. Between 2007 and 2016, she was a senior postdoctoral associate in Guillermo Altenberg’s laboratory at Texas Tech University Health Sciences Center. Her main research interest is to understand the function of proteins, especially membrane proteins, from a biochemical and structural perspective.

Guillermo A. Altenberg

Guillermo A. Altenberg has been the head of the Department of Cell Physiology and Molecular Biophysics at Texas Tech University Health Sciences Center, Lubbock, TX, USA since 2014. He received his MD degree from the School of Medicine of the University of Buenos Aires in Argentina, and his PhD degree from the same university in 1987, working in the Institute for Cardiological Research. He has spent most of his academic career as faculty in the School of Medicine of The University of Texas Medical Branch at Galveston, and has been at Texas Tech University Health Sciences Center since 2007. His research interest is the structure-function of membrane transport proteins, with a focus on spectroscopy and nanotechnology applications.

Received: 2016-09-06

Accepted: 2016-11-02

Published Online: 2017-01-26

Published in Print: 2017-02-01

Citation Information: Nanotechnology Reviews, Volume 6, Issue 1, Pages 33–46, ISSN (Online) 2191-9097, ISSN (Print) 2191-9089, DOI: https://doi.org/10.1515/ntrev-2016-0078.

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