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Protein Science (2004), 13:1832-1840. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Structural conservation in the major facilitator superfamily as revealed by comparative modeling

Eyal Vardy1, Isaiah T. Arkin1, Kay E. Gottschalk2, H. Ronald Kaback3 and Shimon Schuldiner1

1 Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem, 91904 Israel
2 Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
3 Howard Hughes Medical Institute, Departments of Physiology and Microbiology, Immunology, and Molecular Genetics, Molecular Biology Institute, University of California, Los Angeles, California 90095, USA

(RECEIVED January 28, 2004; FINAL REVISION January 28, 2004; ACCEPTED April 7, 2004)



Abstract

The structures of membrane transporters are still mostly unsolved. Only recently, the first two high-resolution structures of transporters of the major facilitator superfamily (MFS) were published. Despite the low sequence similarity of the two proteins involved, lactose permease and glycerol-3-phosphate transporter, the reported structures are highly similar. This leads to the hypothesis that all members of the MFS share a similar structure, regardless of their low sequence identity. To test this hypothesis, we generated models of two other members of the MFS, the Tn10-encoded metal-tetracycline/H+ antiporter (TetAB) and the rat vesicular monoamine transporter (rVMAT2). The models are based on the two MFS structures and on experimental data. The models for both proteins are in good agreement with the data available and support the notion of a shared fold for all MFS proteins.

Keywords: membrane protein; ion-coupled transporters; drug resistance; NEM accessibility

Reprint requests to: Shimon Schuldiner, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem, 91904 Israel; e-mail: Shimon.Schuldiner{at}huji.ac.il; fax: 972-2-5634625.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04657704.


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