[English] 日本語
![](img/lk-miru.gif)
- EMDB-7546: Monomer yeast ATP synthase (F1Fo) reconstituted in nanodisc with ... -
+
Open data
-
Basic information
Entry | Database: EMDB / ID: EMD-7546 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Monomer yeast ATP synthase (F1Fo) reconstituted in nanodisc with inhibitor of oligomycin bound. | |||||||||
![]() | Monomer yeast ATP synthase (F1Fo) reconstituted in nanodisc with inhibitor of oligomycin bound | |||||||||
![]() |
| |||||||||
Function / homology | ![]() cristae formation / mitochondrial proton-transporting ATP synthase, central stalk / : / : / Mitochondrial protein degradation / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase, stator stalk / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) ...cristae formation / mitochondrial proton-transporting ATP synthase, central stalk / : / : / Mitochondrial protein degradation / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase, stator stalk / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial nucleoid / mitochondrial proton-transporting ATP synthase complex / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / photosynthetic electron transport in photosystem I / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / photosynthetic electron transport in photosystem II / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / mitochondrial intermembrane space / ADP binding / protein-containing complex assembly / mitochondrial inner membrane / lipid binding / ATP hydrolysis activity / mitochondrion / ATP binding / identical protein binding / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||
![]() | Srivastava AP / Luo M / Symersky J / Liao MF / Mueller DM | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane. Authors: Anurag P Srivastava / Min Luo / Wenchang Zhou / Jindrich Symersky / Dongyang Bai / Melissa G Chambers / José D Faraldo-Gómez / Maofu Liao / David M Mueller / ![]() Abstract: Mitochondrial adenosine triphosphate (ATP) synthase comprises a membrane embedded F motor that rotates to drive ATP synthesis in the F subunit. We used single-particle cryo-electron microscopy (cryo- ...Mitochondrial adenosine triphosphate (ATP) synthase comprises a membrane embedded F motor that rotates to drive ATP synthesis in the F 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 F c-ring in the direction of ATP synthesis, relative to the structure of isolated F Our cryo-EM structures show how F and F are coupled, give insight into the proton translocation pathway, and show how oligomycin blocks ATP synthesis. | |||||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
-
Downloads & links
-EMDB archive
Map data | ![]() | 116.7 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 28.5 KB 28.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.3 KB | Display | ![]() |
Images | ![]() | 57.3 KB | ||
Others | ![]() | 98.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 569.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 568.6 KB | Display | |
Data in XML | ![]() | 12.2 KB | Display | |
Data in CIF | ![]() | 16.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6cp3MC ![]() 7547C ![]() 7548C ![]() 7549C ![]() 6cp5C ![]() 6cp6C ![]() 6cp7C M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Monomer yeast ATP synthase (F1Fo) reconstituted in nanodisc with inhibitor of oligomycin bound | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.23 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-Additional map: Additional map
File | emd_7546_additional.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Additional map | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
+Entire : Monomer yeast ATP synthase (F1Fo) reconstituted in nanodisc with ...
+Supramolecule #1: Monomer yeast ATP synthase (F1Fo) reconstituted in nanodisc with ...
+Macromolecule #1: ATP synthase subunit 9, mitochondrial
+Macromolecule #2: ATP synthase subunit 5, mitochondrial
+Macromolecule #3: ATP synthase subunit alpha, mitochondrial
+Macromolecule #4: ATP synthase subunit beta, mitochondrial
+Macromolecule #5: ATP synthase subunit gamma, mitochondrial
+Macromolecule #6: ATP synthase subunit delta, mitochondrial
+Macromolecule #7: ATP synthase subunit epsilon, mitochondrial
+Macromolecule #8: ATP synthase subunit 4, mitochondrial
+Macromolecule #9: ATP synthase subunit d, mitochondrial
+Macromolecule #10: ATP synthase subunit H, mitochondrial
+Macromolecule #11: ATP synthase subunit f, mitochondrial
+Macromolecule #12: ATP synthase protein 8
+Macromolecule #13: ATP synthase subunit a
+Macromolecule #14: ATP synthase subunit J, mitochondrial
+Macromolecule #15: ADENOSINE-5'-TRIPHOSPHATE
+Macromolecule #16: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Concentration | 1. mg/mL |
---|---|
Buffer | pH: 8 / Details: 20 mM Tris-HCl, 150 mM NaCl, pH 8.0 |
Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 91 % |
-
Electron microscopy
Microscope | FEI POLARA 300 |
---|---|
Temperature | Min: 80.0 K / Max: 105.0 K |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number real images: 2896 / Average electron dose: 8.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Calibrated defocus max: 2.7 µm / Calibrated defocus min: 1.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.0 mm / Nominal magnification: 31000 |
Sample stage | Specimen holder model: GATAN LIQUID NITROGEN / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Tecnai Polara / Image courtesy: FEI Company |
+
Image processing
-Atomic model buiding 1
Refinement | Space: REAL |
---|---|
Output model | ![]() PDB-6cp3: |