An approach to membrane protein structure without crystals.

Abstract:

: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.

authors

Sorgen PL,Hu Y,Guan L,Kaback HR,Girvin ME

doi

10.1073/pnas.182552199

keywords:

subject

Has Abstract

pub_date

2002-10-29 00:00:00

pages

14037-40

issue

22

eissn

0027-8424

issn

1091-6490

pii

182552199

journal_volume

99

pub_type

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