Structure, substrate binding, and symmetry of the mitochondrial ADP/ATP carrier in its matrix-open state.

ABSTRACT: The mitochondrial ADP/ATP carrier (AAC) performs the first and last step in oxidative phosphorylation by exchanging ADP and ATP across the mitochondrial inner membrane. Its optimal function has been shown to be dependent on cardiolipins (CLs), unique phospholipids located almost exclusively in the mitochondrial membrane. In addition, AAC exhibits an enthralling threefold pseudosymmetry, a unique feature of members of the SLC25 family. Recently, its conformation poised for binding of ATP was solved by x-ray crystallography referred to as the matrix state. Binding of the substrate leads to conformational changes that export of ATP to the mitochondrial intermembrane space. In this contribution, we investigate the influence of CLs on the structure, substrate-binding properties, and structural

SUBMITTER: Montalvo-Acosta JJ 

PROVIDER: S-EPMC8715212 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature