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Structural conservation in the major facilitator superfamily as revealed by comparative modeling
Author(s) -
Vardy Eyal,
Arkin Isaiah T.,
Gottschalk Kay E.,
Kaback H. Ronald,
Schuldiner Shimon
Publication year - 2004
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.04657704
Subject(s) - major facilitator superfamily , lactose permease , transporter , superfamily , permease , computational biology , antiporters , antiporter , biology , membrane transport protein , solute carrier family , biochemistry , chemistry , receptor , gene , membrane
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.