Journal
BIOCHEMICAL JOURNAL
Volume 463, Issue -, Pages 297-307Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20130619
Keywords
membrane protein; protein purification; protein structure; Slc26/SulP; small-angle neutron scattering; transporter
Categories
Funding
- Medical Research Council [G1000054]
- Scottish government/Royal Society of Edinburgh
- Medical Research Council [G1000054] Funding Source: researchfish
- MRC [G1000054] Funding Source: UKRI
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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.
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