Elucidation of the structure and molecular mechanisms of the aspartate antiporter.

ABSTRACT: The transport of compounds across the cell membrane is essential for maintaining cellular homeostasis. Secondary exchange transporters mediate the movement of a wide range of substrates against their concentration gradients by harnessing the energy stored in electrochemical gradients. However, the molecular mechanism of substrate exchange by secondary transporters remains unclear. Here, we determined the structures of the aspartate exchanger AspT from Tetragenococcus halophilus using cryo-EM single-particle analysis and X-ray crystallography. We captured AspT in two distinct conformations: the apo outward-facing state and the substrate (L-Aspartate)-bound partially-open inward-facing intermediate state. AspT functions as a homodimer and comprises three domains: a dimerization domain, a sub

SUBMITTER: Nanatani K 

PROVIDER: S-EPMC12462496 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature