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Science 293 (5536): 1793-1800

Copyright © 2001 by the American Association for the Advancement of Science

Structure of MsbA from E. coli: A Homolog of the Multidrug Resistance ATP Binding Cassette (ABC) Transporters

Geoffrey Chang,* Christopher B. Roth

Multidrug resistance (MDR) is a serious medical problem and presents a major challenge to the treatment of disease and the development of novel therapeutics. ABC transporters that are associated with multidrug resistance (MDR-ABC transporters) translocate hydrophobic drugs and lipids from the inner to the outer leaflet of the cell membrane. To better elucidate the structural basis for the "flip-flop" mechanism of substrate movement across the lipid bilayer, we have determined the structure of the lipid flippase MsbA from Escherichia coli by x-ray crystallography to a resolution of 4.5 angstroms. MsbA is organized as a homodimer with each subunit containing six transmembrane alpha -helices and a nucleotide-binding domain. The asymmetric distribution of charged residues lining a central chamber suggests a general mechanism for the translocation of substrate by MsbA and other MDR-ABC transporters. The structure of MsbA can serve as a model for the MDR-ABC transporters that confer multidrug resistance to cancer cells and infectious microorganisms.

Department of Molecular Biology, MB-9, The Scripps Research Institute, La Jolla, CA 92037, USA.
*   To whom correspondence should be addressed. E-mail: gchang{at}scripps.edu



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S. Samanta, T. Ayvaz, M. Reyes, H. A. Shuman, J. Chen, and A. L. Davidson (2003)
J. Biol. Chem. 278, 35265-35271
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A Structural Model for the Open Conformation of the mdr1 P-glycoprotein Based on the MsbA Crystal Structure.
M. Seigneuret and A. Garnier-Suillerot (2003)
J. Biol. Chem. 278, 30115-30124
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STRUCTURAL BIOLOGY: Enhanced: Breaching the Barrier.
K. P. Locher, R. B. Bass, and D. C. Rees (2003)
Science 301, 603-604
   Abstract »    Full Text »    PDF »
N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits.
K. W. Chan, H. Zhang, and D. E. Logothetis (2003)
EMBO J. 22, 3833-3843
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ATP-Dependent Transport of Bile Acid Intermediates across Rat Liver Peroxisomal Membranes.
M. Une, Y. Iguchi, T. Sakamoto, T. Tomita, Y. Suzuki, M. Morita, and T. Imanaka (2003)
J. Biochem. 134, 225-230
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The Dynamic Dimerization of the Yeast ADP/ATP Carrier in the Inner Mitochondrial Membrane Is Affected by Conserved Cysteine Residues.
S. D. Dyall, S. C. Agius, C. De Marcos Lousa, V. Trezeguet, and K. Tokatlidis (2003)
J. Biol. Chem. 278, 26757-26764
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The ATP Hydrolysis Cycle of the Nucleotide-binding Domain of the Mitochondrial ATP-binding Cassette Transporter Mdl1p.
E. Janas, M. Hofacker, M. Chen, S. Gompf, C. van der Does, and R. Tampe (2003)
J. Biol. Chem. 278, 26862-26869
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Translocation of Phospholipids Is Facilitated by a Subset of Membrane-spanning Proteins of the Bacterial Cytoplasmic Membrane.
M. A. Kol, A. van Dalen, A. I. P. M. de Kroon, and B. de Kruijff (2003)
J. Biol. Chem. 278, 24586-24593
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P-glycoprotein Catalytic Mechanism: STUDIES OF THE ADP-VANADATE INHIBITED STATE.
I. L. Urbatsch, G. A. Tyndall, G. Tombline, and A. E. Senior (2003)
J. Biol. Chem. 278, 23171-23179
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ABCA1-Deficient Mice: Insights Into the Role of Monocyte Lipid Efflux in HDL Formation and Inflammation.
R. J. Aiello, D. Brees, and O. L. Francone (2003)
Arterioscler Thromb Vasc Biol 23, 972-980
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A missense mutation in the Abcg5 gene causes phytosterolemia in SHR, stroke-prone SHR, and WKY rats.
K. A. Scoggan, H. Gruber, and K. Lariviere (2003)
J. Lipid Res. 44, 911-916
   Abstract »    Full Text »    PDF »
CFTR directly mediates nucleotide-regulated glutathione flux.
I. Kogan, M. Ramjeesingh, C. Li, J. F. Kidd, Y. Wang, E. M. Leslie, S. P. C. Cole, and C. E. Bear (2003)
EMBO J. 22, 1981-1989
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