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

Heinrich Jung1

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

FEBS Letters
|October 2, 2002
PubMed
Summary

The sodium/substrate symporter family (SSSF) transports vital molecules across cell membranes. Ligand-induced structural changes suggest an ordered mechanism for sodium and substrate binding during transport.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • The sodium/substrate symporter family (SSSF) comprises transporters crucial for cellular uptake of diverse solutes like sugars, amino acids, and ions.
  • These symporters are found in both prokaryotic and eukaryotic organisms, highlighting their fundamental biological role.
  • Previous studies suggest a common structural motif of 13 transmembrane domains in SSSF proteins.

Purpose of the Study:

  • To elucidate the structural and mechanistic aspects of sodium/substrate symporter function.
  • To identify key regions involved in solute and sodium binding within SSSF proteins.
  • To investigate the dynamic structural changes occurring upon ligand binding.

Main Methods:

  • Bioinformatic analysis of SSSF protein topology to determine transmembrane domains.

Related Experiment Videos

  • Identification of potential sodium and substrate binding sites through sequence and structural analysis.
  • Application of protein chemical and spectroscopic techniques to study ligand-induced conformational changes.

    • Main Results:

    • A conserved topology of 13 transmembrane domains was proposed for SSSF proteins.
    • Specific regions critical for sodium and/or substrate binding were identified.
    • Spectroscopic data revealed ligand-induced structural alterations, indicating close proximity between binding sites.

    Conclusions:

    • The findings support a model where sodium and substrate binding sites are closely interacting within SSSF proteins.
    • Ligand binding induces conformational changes consistent with an ordered binding mechanism for transport.
    • This research provides insights into the molecular mechanism of a vital class of membrane transporters.