Low resolution structure of a bacterial SLC26 transporter reveals dimeric stoichiometry and mobile intracellular domains.

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

SUBMITTER: Compton EL 

PROVIDER: S-EPMC3143664 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature