Structural conservation in the major facilitator superfamily as revealed by comparative modeling.
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.
Vardy
Eyal
E
Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem, 91904 Israel.
Arkin
Isaiah T
IT
Gottschalk
Kay E
KE
Kaback
H Ronald
HR
Schuldiner
Shimon
S
D000818:Animals; D017920:Antiporters / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003198:Computer Simulation; D008562:Membrane Glycoproteins / Q000737:chemistry*; D026901:Membrane Transport Proteins / Q000737:chemistry*; D051381:Rats; D040681:Structural Homology, Protein; D050492:Vesicular Biogenic Amine Transport Proteins; D050493:Vesicular Monoamine Transport Proteins
D017920:Antiporters; D001426:Bacterial Proteins; D008562:Membrane Glycoproteins; D026901:Membrane Transport Proteins; D050492:Vesicular Biogenic Amine Transport Proteins; D050493:Vesicular Monoamine Transport Proteins; C079051:tetA protein, Bacteria