Reports

Structure of the Multidrug Transporter EmrD from Escherichia coli

Yong Yin,^* Xiao He,^* Paul Szewczyk, That Nguyen, Geoffrey Chang

EmrD is a multidrug transporter from the Major Facilitator Superfamily that expels amphipathic compounds across the inner membrane of Escherichia coli. Here, we report the x-ray structure of EmrD determined to a resolution of 3.5 angstroms. The structure reveals an interior that is composed mostly of hydrophobic residues, which is consistent with its role transporting amphipathic molecules. Two long loops extend into the inner leaflet side of the cell membrane. This region can serve to recognize and bind substrate directly from the lipid bilayer. We propose that multisubstrate specificity, binding, and transport are facilitated by these loop regions and the internal cavity.

The Scripps Research Institute, Department of Molecular Biology, 10550 North Torrey Pines Road, CB-105, La Jolla, CA 92037, USA.

^* These authors contributed equally to this work.

To whom correspondence should be addressed. E-mail: gchang{at}scripps.edu

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Interactions between Phosphatidylethanolamine Headgroup and LmrP, a Multidrug Transporter: A CONSERVED MECHANISM FOR PROTON GRADIENT SENSING?.

P. Hakizimana, M. Masureel, B. Gbaguidi, J.-M. Ruysschaert, and C. Govaerts (2008)
J. Biol. Chem. 283, 9369-9376
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Analysis of Tryptophan Residues in the Staphylococcal Multidrug Transporter QacA Reveals Long-Distance Functional Associations of Residues on Opposite Sides of the Membrane.

K. A. Hassan, T. Souhani, R. A. Skurray, and M. H. Brown (2008)
J. Bacteriol. 190, 2441-2449
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Sugar binding induces an outward facing conformation of LacY.

I. Smirnova, V. Kasho, J.-Y. Choe, C. Altenbach, W. L. Hubbell, and H. R. Kaback (2007)
PNAS 104, 16504-16509
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Structural determination of wild-type lactose permease.

L. Guan, O. Mirza, G. Verner, S. Iwata, and H. R. Kaback (2007)
PNAS 104, 15294-15298
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Docking and homology modeling explain inhibition of the human vesicular glutamate transporters.

J. Almqvist, Y. Huang, A. Laaksonen, D.-N. Wang, and S. Hovmoller (2007)
Protein Sci. 16, 1819-1829
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The yeast mitochondrial ADP/ATP carrier functions as a monomer in mitochondrial membranes.

L. Bamber, M. Harding, M. Monne, D.-J. Slotboom, and E. R. S. Kunji (2007)
PNAS 104, 10830-10834
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A genomic strategy for cloning, expressing and purifying efflux proteins of the major facilitator superfamily.

G. Szakonyi, D. Leng, P. Ma, K. E. Bettaney, M. Saidijam, A. Ward, S. Zibaei, A. T. Gardiner, R. J. Cogdell, P. Butaye, et al. (2007)
J. Antimicrob. Chemother. 59, 1265-1270
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Identification by Comprehensive Chimeric Analysis of a Key Residue Responsible for High Affinity Glucose Transport by Yeast HXT2.

T. Kasahara, M. Maeda, M. Ishiguro, and M. Kasahara (2007)
J. Biol. Chem. 282, 13146-13150
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Emulating Membrane Protein Evolution by Rational Design.

M. Rapp, S. Seppala, E. Granseth, and G. von Heijne (2007)
Science 315, 1282-1284
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Interactions among PIN-FORMED and P-Glycoprotein Auxin Transporters in Arabidopsis.

J. J. Blakeslee, A. Bandyopadhyay, O. R. Lee, J. Mravec, B. Titapiwatanakun, M. Sauer, S. N. Makam, Y. Cheng, R. Bouchard, J. Adamec, et al. (2007)
PLANT CELL 19, 131-147
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Yeast mitochondrial ADP/ATP carriers are monomeric in detergents.

L. Bamber, M. Harding, P. J. G. Butler, and E. R. S. Kunji (2006)
PNAS 103, 16224-16229
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