Structural conservation in the major facilitator superfamily as revealed by comparative modeling

Eyal Vardy, Isaiah T. Arkin, Kay E. Gottschalk, H. Ronald Kaback, Shimon Schuldiner*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

89 Scopus citations


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.

Original languageAmerican English
Pages (from-to)1832-1840
Number of pages9
JournalProtein Science
Issue number7
StatePublished - Jul 2004


  • Drug resistance
  • Ion-coupled transporters
  • Membrane protein
  • NEM accessibility


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