Justin D Walter / Marta Sawicka / Raimund Dutzler /
PubMed Abstract
The epithelial anion transporter SLC26A9 contributes to airway surface hydration and gastric acid production. Colocalizing with CFTR, SLC26A9 has been proposed as a target for the treatment of cystic ...The epithelial anion transporter SLC26A9 contributes to airway surface hydration and gastric acid production. Colocalizing with CFTR, SLC26A9 has been proposed as a target for the treatment of cystic fibrosis. To provide molecular details of its transport mechanism, we present cryo-EM structures and a functional characterization of murine Slc26a9. These structures define the general architecture of eukaryotic SLC26 family members and reveal an unusual mode of oligomerization which relies predominantly on the cytosolic STAS domain. Our data illustrates conformational transitions of Slc26a9, supporting a rapid alternate-access mechanism which mediates uncoupled chloride transport with negligible bicarbonate or sulfate permeability. The characterization of structure-guided mutants illuminates the properties of the ion transport path, including a selective anion binding site located in the center of a mobile module within the transmembrane domain. This study thus provides a structural foundation for the understanding of the entire SLC26 family and potentially facilitates their therapeutic exploitation.
EMDB-4997:Cryo-EM density of murine Solute Carrier 26 family member A9 (Slc26a9) anion transporter in the inward-facing state PDB-6rtc:Structure of murine Solute Carrier 26 family member A9 (Slc26a9) anion transporter in the inward-facing state Method: EM (single particle) / Resolution: 3.96 Å
EMDB-4998:Cryo-EM density of murine Solute Carrier 26 family member A9 (Slc26a9) anion transporter in an intermediate state PDB-6rtf:Structure of murine Solute Carrier 26 family member A9 (Slc26a9) anion transporter in an intermediate state Method: EM (single particle) / Resolution: 7.77 Å
Source
mus musculus (house mouse)
Keywords
MEMBRANE PROTEIN / SLC26 family / anion transporter / membrane protein structure / transport mechanism / cryo-EM / single particle
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