ArticleThe Journal of biological chemistry2011
Low resolution structure of a bacterial SLC26 transporter reveals dimeric stoichiometry and mobile intracellular domains.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 45 citations in OpenAlex.
- STAS Domain Only Proteins in Bacterial Gene Regulation.Frontiers in cellular and infection microbiology · 2021Review
- Engineered Accumulation of Bicarbonate in Plant Chloroplasts: Known Knowns and Known Unknowns.Frontiers in plant science · 2021Review
- Structural mechanism of the active bicarbonate transporter from cyanobacteria.Nature plants · 2019Article
- Structural basis for functional interactions in dimers of SLC26 transporters.Nature communications · 2019Article
- Importance of SLC26 Transmembrane Anion Exchangers in Sperm Post-testicular Maturation and Fertilization Potential.Frontiers in cell and developmental biology · 2019Review
- Structural modeling of an outer membrane electron conduit from a metal-reducing bacterium suggests electron transfer via periplasmic redox partners.The Journal of biological chemistry · 2018Article
- Low-Resolution Structure of Detergent-Solubilized Membrane Proteins from Small-Angle Scattering Data.Biophysical journal · 2017Article
- The E. coli dicarboxylic acid transporters DauA act as a signal transducer by interacting with the DctA uptake system.Scientific reports · 2017Article
- Membrane Association Landscape of Myelin Basic Protein Portrays Formation of the Myelin Major Dense Line.Scientific reports · 2017Article
- Extracellular Cl(-) regulates human SO4 (2-)/anion exchanger SLC26A1 by altering pH sensitivity of anion transport.Pflugers Archiv : European journal of physiology · 2016Article
- Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family.Nature structural & molecular biology · 2015Article
- Mechanism and synergism in epithelial fluid and electrolyte secretion.Pflugers Archiv : European journal of physiology · 2014Review
- Probing the conformation of FhaC with small-angle neutron scattering and molecular modeling.Biophysical journal · 2014Article
- Assessing the conformational changes of pb5, the receptor-binding protein of phage T5, upon binding to its Escherichia coli receptor FhuA.The Journal of biological chemistry · 2013Article
- The conserved tetrameric subunit stoichiometry of Slc26 proteins.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2013Article
- Small angle neutron scattering for the study of solubilised membrane proteins.The European physical journal. E, Soft matter · 2013Review
- Characterization of SLCO5A1/OATP5A1, a solute carrier transport protein with non-classical function.PloS one · 2013Article
- CFTR-SLC26 transporter interactions in epithelia.Biophysical reviews · 2012Article
- Solute carrier family 26 member a2 (Slc26a2) protein functions as an electroneutral SOFormula/OH-/Cl- exchanger regulated by extracellular Cl-.The Journal of biological chemistry · 2012Article
- STAS domain structure and function.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2011Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The SLC26/SulP (solute carrier/sulfate transporter) proteins are a superfamily of anion transporters conserved from bacteria to man, of which four have been identified in human diseases. Proteins within the SLC26/SulP family exhibit a wide variety of functions, transporting anions from halides to carboxylic acids. The proteins comprise a transmembrane domain containing between 10-12 transmembrane helices followed a by C-terminal cytoplasmic sulfate transporter and anti-sigma factor antagonist (STAS) domain. These proteins are expected to undergo conformational changes during the transport cycle; however, structural information for this family remains sparse, particularly for the full-length proteins. To address this issue, we conducted an expression and detergent screen on bacterial Slc26 proteins. The screen identified a Yersinia enterocolitica Slc26A protein as the ideal candidate for further structural studies as it can be purified to homogeneity. Partial proteolysis, co-purification, and analytical size exclusion chromatography demonstrate that the protein purifies as stable oligomers. Using small angle neutron scattering combined with contrast variation, we have determined the first low resolution structure of a bacterial Slc26 protein without spectral contribution from the detergent. The structure confirms that the protein forms a dimer stabilized via its transmembrane core; the cytoplasmic STAS domain projects away from the transmembrane domain and is not involved in dimerization. Supported by additional biochemical data, the structure suggests that large movements of the STAS domain underlie the conformational changes that occur during transport.
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