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Structural biology

It's not all in the family

Nature volume 454, pages 593–594 (2008)Cite this article

There are no sequential snapshots of a transporter protein as it mediates the simultaneous passage of ions and solutes into a cell. Comparing different snapshots of structurally related transporters offers fascinating insights.

Ion-coupled transporters are molecular machines that allow the passage of specific solutes, such as nutrients and neurotransmitters, across the cell membrane by transferring them together with one or more cations, often sodium ions. The energy released as these cations move into the cell down their concentration gradient is used to power the 'uphill' movement of the solute. For proper function, the transporter, which is embedded in the cell membrane, must alternately expose a binding site at either side of the membrane, capturing its cargo on one side and releasing it on the other — a principle called alternating access. In recent years, the structures of several ion-coupled transporters have been resolved, but in only a single conformation during transport. If we are to understand the molecular mechanism underlying transport, we need to know the structure of the transporter in different conformations. Faham et al.1 take an initial, rather unexpected, step towards this goal by documenting in Science the first crystal structure of the sodium-coupled galactose transporter vSGLT.

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Figure 1: The entrance and exit routes through the vSGLT transporter.

References

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Authors and Affiliations

  1. Baruch I. Kanner is in the Department of Biochemistry, Hebrew University Hadassah Medical School, Jerusalem 91120, Israel. kannerb@cc.huji.ac.il,

    Baruch I. Kanner

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  1. Baruch I. Kanner
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Kanner, B. It's not all in the family. Nature 454, 593–594 (2008). https://doi.org/10.1038/454593a

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