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