Membrane topology of the electrogenic aspartate-alanine antiporter AspT of Tetragenococcus halophilus

Biochem Biophys Res Commun. 2005 Mar 4;328(1):20-6. doi: 10.1016/j.bbrc.2004.12.133.

Abstract

AspT is an electrogenic aspartate:alanine exchange protein that represents the vectorial component of a proton-motive metabolic cycle found in some strains of Tetragenococcus halophilus. AspT is the sole member of a new family, the Aspartate: Alanine Exchanger (AAE) family, in secondary transporters, according to the computational classification proposed by Saier et al. (http://www.biology.ucsd.edu/~msaier/transport/). We analyzed the topology of AspT biochemically, by using fusion methods in combination with alkaline phosphatase or beta-lactamase. These results suggested that AspT has a unique topology; 8 TMS, a large cytoplasmic loop (183 amino acids) between TMS5 and TMS6, and N- and C-termini that both face the periplasm. These results demonstrated a unique 2D-structure of AspT as the novel AAE family.

MeSH terms

  • Amino Acid Sequence
  • Antiporters / chemistry*
  • Antiporters / genetics
  • Antiporters / metabolism*
  • Cell Membrane / chemistry*
  • Cell Membrane / metabolism*
  • Enterococcus / chemistry*
  • Enterococcus / metabolism*
  • Escherichia coli / chemistry
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Models, Biological*
  • Molecular Sequence Data
  • Protein Conformation
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Structure-Activity Relationship

Substances

  • Antiporters
  • Recombinant Fusion Proteins