An approach to membrane protein structure without crystals

作者：Sorgen PL; Hu YL; Guan L; Kaback HR^*; Girvin ME

来源：Proceedings of the National Academy of Sciences, 2002, 99(22): 14037-14040.

DOI：10.1073/pnas.182552199

• bioenergetics
• membrane transport
• lactose permease
• site-directed thiol cross-linking
• engineered divalent metal-binding sites

The lactose permease of Escherichia coli catalyzes coupled translocation of galactosides, and H+ across the cell membrane. It is the best-characterized member of the Major Facilitator Superfamily, a related group of membrane proteins with 12 transmembrane domains that mediate transport of various substrates across cell membranes. Despite decades of effort and their functional importance in all kingdoms of life, no high-resolution structures have been solved for any member of this family. However, extensive biochemical, genetic, and biophysical studies on lactose permease have established its transmembrane topology, secondary structure, and numerous interhelical contacts. Here we demonstrate that this information is sufficient to calculate a structural model at the level of helix packing or better.

• 出版日期2002-10-29