The inward-open and outward-open structures of MjNhaP1 explain the mechanism of electroneutral sodium-proton antiport across the cell membrane.

Sodium ions but not protons induce defined helix movements in a sodium/proton antiporter and suggest a mechanism for Na + binding and transport.

The X-ray structure of the PaNhaP provides a unique view of substrate-ion binding and release in electroneutral sodium/proton antiporters.

Ptch1/2 can lower the sensitivity of Smo to activation by Shh via the secretion of a sterol precursor.

Structure of the Mrp antiporter, an ancestor of respiratory complex I, suggests a mechanism of coupling between cation and proton translocation, applicable to a large family of related membrane proteins.

Cis-regulation such as enhancers and promoters plays a major role in parallel gene expression divergence and has features that make it a well-poised substrate for adaptive evolution.

Structures of CysZ show a antiparallel membrane protein with an unanticipated fold and together with functional characterization provide insight into a bacterial sulfate translocating system.

The high-resolution x-ray structure of an asymmetrical SeCitS dimer, present in the inward- and outward-facing state, provides a complete mechanism of substrate and ion translocation in a sodium-dependent symporter.

Structures of multiple states of two dicarboxylate transporters explain the conformational changes needed for substrate import.

The structure of the membrane-integrated components of a unique substrate decarboxylation-driven primary-active sodium pump provides insights into its transport mechanism.