title: Conserved structure and domain organization among bacterial Slc26 transporters.
abstract: 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.
authors.affiliation: *College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
authors.forename: Emma L R
authors.initials: EL
authors.lastname: Compton
authors.affiliation: *College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
authors.forename: Kimberly
authors.initials: K
authors.lastname: Page
authors.affiliation: †School of Biochemistry, University of Bristol, Bristol BS8 1TD, U.K.
authors.forename: Heather E
authors.initials: HE
authors.lastname: Findlay
authors.affiliation: ‡The Deuteration Laboratory, Institut Laue-Langevin, CIBB, 6 rue Jules Horowitz, 38042 Grenoble cedex 9, France.
authors.forename: Michael
authors.initials: M
authors.lastname: Haertlein
authors.affiliation: ‡The Deuteration Laboratory, Institut Laue-Langevin, CIBB, 6 rue Jules Horowitz, 38042 Grenoble cedex 9, France.
authors.forename: Martine
authors.initials: M
authors.lastname: Moulin
authors.affiliation: *College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
authors.forename: Ulrich
authors.initials: U
authors.lastname: Zachariae
authors.affiliation: *College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
authors.forename: David G
authors.initials: DG
authors.lastname: Norman
authors.affiliation: §Institut de Biologie Structurale CEA, CNRS, UJF, 41 rue Jules Horowitz, 38027 Grenoble, France.
authors.forename: Frank
authors.initials: F
authors.lastname: Gabel
authors.forename: Arnaud
authors.initials: A
authors.lastname: Javelle
mesh_terms: D027321:Anion Transport Proteins / Q000737:chemistry* / Q000235:genetics; D001419:Bacteria / Q000737:chemistry / Q000145:classification / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D017124:Conserved Sequence; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D053838:Scattering, Small Angle; D015008:Yersinia enterocolitica / Q000737:chemistry* / Q000235:genetics
chemical_list: D027321:Anion Transport Proteins; D001426:Bacterial Proteins