EMD-7549

Single-particle
4.1 Å
EMD-7549 Deposition: 13/03/2018
Map released: 11/04/2018
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-7549

Monomer yeast ATP synthase Fo reconstituted in nanodisc generated from masked refinement.

EMD-7549

Single-particle
4.1 Å
EMD-7549 Deposition: 13/03/2018
Map released: 11/04/2018
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sample: Monomer yeast ATP synthase Fo reconstituted in nanodisc generated from masked refinement.
Fitted models: 6cp7 (Avg. Q-score: 0.311)

Deposition Authors: Srivastava AP , Luo M
High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane.
PUBMED: 29650704
DOI: doi:10.1126/science.aas9699
ISSN: 1095-9203
ASTM: SCIEAS
Abstract:
Mitochondrial adenosine triphosphate (ATP) synthase comprises a membrane embedded Fo motor that rotates to drive ATP synthesis in the F1 subunit. We used single-particle cryo-electron microscopy (cryo-EM) to obtain structures of the full complex in a lipid bilayer in the absence or presence of the inhibitor oligomycin at 3.6- and 3.8-angstrom resolution, respectively. To limit conformational heterogeneity, we locked the rotor in a single conformation by fusing the F6 subunit of the stator with the δ subunit of the rotor. Assembly of the enzyme with the F6-δ fusion caused a twisting of the rotor and a 9° rotation of the Fo c10-ring in the direction of ATP synthesis, relative to the structure of isolated Fo Our cryo-EM structures show how F1 and Fo are coupled, give insight into the proton translocation pathway, and show how oligomycin blocks ATP synthesis.