Conserved structure and domain organization among bacterial Slc26 transporters
Compton-Daw, Emma and Page, Kimberly and Findlay, Heather E. and Haertlein, Michael and Moulin, Martine and Zachariae, Ulrich and Norman, David G. and Gabel, Frank and Javelle, Arnaud (2014) Conserved structure and domain organization among bacterial Slc26 transporters. Biochemical Journal, 463 (2). pp. 297-307. ISSN 0264-6021 (https://doi.org/10.1042/BJ20130619)
Preview |
Text.
Filename: Compton_etal_BJ2014_structure_and_domain_organisation_amongst_bacterial_Slc26_transporters.pdf
Accepted Author Manuscript Download (819kB)| Preview |
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.
ORCID iDs
Compton-Daw, Emma ORCID: https://orcid.org/0000-0002-3832-7194, Page, Kimberly, Findlay, Heather E., Haertlein, Michael, Moulin, Martine, Zachariae, Ulrich, Norman, David G., Gabel, Frank and Javelle, Arnaud ORCID: https://orcid.org/0000-0002-3611-5737;-
-
Item type: Article ID code: 52281 Dates: DateEvent15 October 2014Published17 July 2014Published Online17 July 2014AcceptedNotes: The final version of record is available at http://www.biochemj.org/bj/463/bj4630297.htm Subjects: Medicine > Pharmacy and materia medica Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Professional Services > Human Resources DirectorateDepositing user: Pure Administrator Date deposited: 31 Mar 2015 07:19 Last modified: 11 Nov 2024 11:01 Related URLs: URI: https://strathprints.strath.ac.uk/id/eprint/52281