Membrane plasticity facilitates recognition of the inhibitor oligomycin by the mitochondrial ATP synthase rotor.

ABSTRACT: Enzymes in the respiratory chain are increasingly seen as potential targets against multi-drug resistance of human pathogens and cancerous cells. However, a detailed understanding of the mechanism and specificity determinants of known inhibitors is still lacking. Oligomycin, for example, has been known to be an inhibitor of the membrane motor of the mitochondrial ATP synthase for over five decades, and yet little is known about its mode of action at the molecular level. In a recent breakthrough, a crystal structure of the S. cerevisiae c-subunit ring with bound oligomycin revealed the inhibitor docked on the outer face of the proton-binding sites, deep into the transmembrane region. However, the structure of the complex was obtained in an organic solvent rather than detergent or a lipid bi

SUBMITTER: Zhou W 

PROVIDER: S-EPMC6176861 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature