EMD-7549
Monomer yeast ATP synthase Fo reconstituted in nanodisc generated from masked refinement.
EMD-7549
Single-particle4.1 Å
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Map released: 11/04/2018
Last modified: 23/10/2024
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
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
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High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane.
Srivastava AP
,
Luo M
,
Zhou W
,
Symersky J,
Bai D,
Chambers MG
,
Faraldo-Gomez JD
,
Liao M
,
Mueller DM
(2018) Science , 360
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(2018) Science , 360
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.
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.