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Comment
. 2008 Aug 8;321(5890):781-2.
doi: 10.1126/science.1161495.

Structural biology. Symmetric transporters for asymmetric transport

Nathan K Karpowich  1 , Da-Neng Wang
Affiliations
Comment

Structural biology. Symmetric transporters for asymmetric transport

Nathan K Karpowich et al. Science. .
No abstract available

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Figures

Figure
Figure. Gated Pores and Rocker Switches
(A) Net sugar transport across the intestinal epithelia is catalyzed by SGLT1 in the apical membrane, which couples Na+ influx down its concentration gradient to glucose uptake, and GLUT2, which facilitates glucose transport across the membrane to the basal side of the cell. A similar transport pathway is responsible for glucose reabsorption in the kidneys. Gated pores like SGLT1 are formed by the association of two V-shaped domains intertwined in an antiparallel manner. In contrast, two parallel helical bundles associate to form a shared binding site at their interface in rocker switch GLUT2, a MFS protein. (B) In gated pores such as SGLT1, the rotation of two broken helices permits alternating access of the substrates to the opposing sides of the membrane, as seen by comparison of the vSGLT and LeuT structures. Rocker switches, exemplified by the glycerol-3-phosphate transporter (GlpT) (5) here, are thought to function by the rotation of two domains towards one another, alternately exposing the substrate-binding site to each side of the membrane. The field anxiously awaits the visualization of a rocker switch in its Co state.
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