Conformational changes in the yeast mitochondrial ABC transporter Atm1 during the transport cycle
Thomas L. Ellinghaus, Thomas Marcellino, Vasundara Srinivasan, Roland Lill, Werner Kühlbrandt
Abstract
showed a tight association of the two nucleotide-binding domains, a rearrangement of the C-terminal helices, and closure of the putative substrate-binding cavity in the homodimeric transporter. We identified a hydrophobic patch on the C-terminal helices of yeast Atm1, which is unique among type IV ABC transporters of known structure. Truncation mutants of yeast Atm1 suggest that the C-terminal helices stabilize the dimer, yet are not necessary for closure of the nucleotide-binding domains.
Topics & Concepts
ATP-binding cassette transporterYeastNucleotideDimerTransporterSaccharomyces cerevisiaeBiochemistryTransport proteinTransmembrane domainChemistryCytosolBiogenesisConformational changeElectron transport chainBiophysicsBiologyCrystallographyMembraneEnzymeGeneOrganic chemistryTrace Elements in HealthRNA and protein synthesis mechanismsIron Metabolism and Disorders