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FEBS Lett. 2002 Oct 2;529(1):73-7.

The sodium/substrate symporter family: structural and functional features.

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1
Universität Osnabrück, Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, D-49069, Osnabrück, Germany. jung_h@biologie.uni-osnabrueck.de

Abstract

Members of the sodium/substrate symporter family (SSSF, TC 2.A.21) catalyze the uptake of a wide variety of solutes including sugars, proline, pantothenate, and iodide into cells of pro- and eukaryotic origin. Extensive analyses of the topology of different SSSF proteins suggest an arrangement of 13 transmembrane domains as a common topological motif. Regions involved in sodium and/or substrate binding were identified. Furthermore, protein chemical and spectroscopic studies reveal ligand-induced structural alterations which are consistent with close interactions between the sites of sodium and substrate binding, thereby supporting an ordered binding mechanism for transport.

PMID:
12354616
[Indexed for MEDLINE]
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