Conserved structure and domain organization among bacterial Slc26 transporters

Emma L. R. Compton, Kimberly Page, Heather E. Findlay, Michael Haertlein, Martine Moulin, Ulrich Zachariae, David G. Norman, Frank Gabel, Arnaud Javelle (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


The Slc26 proteins are a ubiquitous superfamily of anion transporters conserved from bacteria to humans, among which four have been identified as human disease genes. Our functional knowledge of this protein family has increased but limited structural information is available. These proteins contain a transmembrane (TM) domain and a C-terminal cytoplasmic sulfate transporter and anti-sigma factor (STAS) domain. In a fundamental step towards understanding the structure/function relationships within the family we have used small-angle neutron scattering (SANS) on two distantly related bacterial homologues to show that there is a common, dimeric and structural architecture among Slc26A transporters. Pulsed electron-electron double resonance (PELDOR) spectroscopy supports the dimeric SANS-derived model. Using chimaeric/truncated proteins we have determined the domain organization: the STAS domains project away from the TM core and are essential for protein stability. We use the SANS-generated envelopes to assess a homology model of the TM core.
Original languageEnglish
Pages (from-to)297-307
Number of pages11
JournalBiochemical Journal
Issue number2
Early online date17 Jul 2014
Publication statusPublished - 15 Oct 2014


  • Anion Transport Proteins
  • Bacteria
  • Bacterial Proteins
  • Conserved Sequence
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Phylogeny
  • Protein Stability
  • Protein Structure, Tertiary
  • Scattering, Small Angle
  • Yersinia enterocolitica


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