[English] 日本語
Yorodumi- EMDB-25963: Yeast ATP synthase State 1catalytic(f) with 10 mM ATP backbone model -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-25963 | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Yeast ATP synthase State 1catalytic(f) with 10 mM ATP backbone model | ||||||||||||
Map data | Unsharpened map. | ||||||||||||
Sample |
| ||||||||||||
Keywords | F1-ATPase / ATP Synthase / Hydrolase / Nanomotor / Complex | ||||||||||||
Function / homology | Function and homology information : / : / : / cristae formation / Mitochondrial protein degradation / mitochondrial proton-transporting ATP synthase complex assembly / : / : / : / : ...: / : / : / cristae formation / Mitochondrial protein degradation / mitochondrial proton-transporting ATP synthase complex assembly / : / : / : / : / : / mitochondrial nucleoid / proton motive force-driven ATP synthesis / proton motive force-driven mitochondrial ATP synthesis / proton transmembrane transporter activity / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / proton transmembrane transport / ADP binding / mitochondrial intermembrane space / protein-containing complex assembly / mitochondrial inner membrane / lipid binding / ATP hydrolysis activity / mitochondrion / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.3 Å | ||||||||||||
Authors | Guo H / Rubinstein JL | ||||||||||||
Funding support | Canada, 3 items
| ||||||||||||
Citation | Journal: Nat Commun / Year: 2022 Title: Structure of ATP synthase under strain during catalysis. Authors: Hui Guo / John L Rubinstein / Abstract: ATP synthases are macromolecular machines consisting of an ATP-hydrolysis-driven F motor and a proton-translocation-driven F motor. The F and F motors oppose each other's action on a shared rotor ...ATP synthases are macromolecular machines consisting of an ATP-hydrolysis-driven F motor and a proton-translocation-driven F motor. The F and F motors oppose each other's action on a shared rotor subcomplex and are held stationary relative to each other by a peripheral stalk. Structures of resting mitochondrial ATP synthases revealed a left-handed curvature of the peripheral stalk even though rotation of the rotor, driven by either ATP hydrolysis in F or proton translocation through F, would apply a right-handed bending force to the stalk. We used cryoEM to image yeast mitochondrial ATP synthase under strain during ATP-hydrolysis-driven rotary catalysis, revealing a large deformation of the peripheral stalk. The structures show how the peripheral stalk opposes the bending force and suggests that during ATP synthesis proton translocation causes accumulation of strain in the stalk, which relaxes by driving the relative rotation of the rotor through six sub-steps within F, leading to catalysis. #1: Journal: Biorxiv / Year: 2022 Title: Structure of ATP synthase under strain during catalysis Authors: Guo H / Rubinstein JL | ||||||||||||
History |
|
-Structure visualization
Supplemental images |
---|
-Downloads & links
-EMDB archive
Map data | emd_25963.map.gz | 31.9 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-25963-v30.xml emd-25963.xml | 32.3 KB 32.3 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_25963_fsc.xml | 8.5 KB | Display | FSC data file |
Images | emd_25963.png | 48.4 KB | ||
Masks | emd_25963_msk_1.map | 64 MB | Mask map | |
Filedesc metadata | emd-25963.cif.gz | 8 KB | ||
Others | emd_25963_half_map_1.map.gz emd_25963_half_map_2.map.gz | 59.4 MB 59.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-25963 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-25963 | HTTPS FTP |
-Validation report
Summary document | emd_25963_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
---|---|---|---|---|
Full document | emd_25963_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | emd_25963_validation.xml.gz | 16.5 KB | Display | |
Data in CIF | emd_25963_validation.cif.gz | 21.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-25963 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-25963 | HTTPS FTP |
-Related structure data
Related structure data | 7tkbMC 7tjsC 7tjtC 7tjuC 7tjvC 7tjwC 7tjxC 7tjyC 7tjzC 7tk0C 7tk1C 7tk2C 7tk3C 7tk4C 7tk5C 7tk6C 7tk7C 7tk8C 7tk9C 7tkaC 7tkcC 7tkdC 7tkeC 7tkfC 7tkgC 7tkhC 7tkiC 7tkjC 7tkkC 7tklC 7tkmC 7tknC 7tkoC 7tkpC 7tkqC 7tkrC 7tksC M: atomic model generated by this map C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|---|
Related items in Molecule of the Month |
-Map
File | Download / File: emd_25963.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Unsharpened map. | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.3475 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Mask #1
File | emd_25963_msk_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #2
File | emd_25963_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #1
File | emd_25963_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Sample components
+Entire : Yeast ATP synthase State 1catalytic(f) with 10 mM ATP backbone model
+Supramolecule #1: Yeast ATP synthase State 1catalytic(f) with 10 mM ATP backbone model
+Macromolecule #1: ATP synthase subunit 9, mitochondrial
+Macromolecule #2: ATP synthase subunit alpha
+Macromolecule #3: ATP synthase subunit beta
+Macromolecule #4: ATP synthase subunit gamma
+Macromolecule #5: ATP synthase subunit delta
+Macromolecule #6: ATP synthase subunit epsilon
+Macromolecule #7: ATP synthase subunit 5
+Macromolecule #8: ATP synthase subunit a
+Macromolecule #9: ATP synthase subunit 4
+Macromolecule #10: ATP synthase subunit d
+Macromolecule #11: ATP synthase subunit f
+Macromolecule #12: ATP synthase subunit H
+Macromolecule #13: ATP synthase subunit J
+Macromolecule #14: ATP synthase protein 8
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 15 mg/mL |
---|---|
Buffer | pH: 7.4 |
Grid | Model: Homemade / Material: COPPER/RHODIUM / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY / Support film - Film thickness: 35 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 120 sec. |
Vitrification | Cryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: LEICA EM GP |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number real images: 10037 / Average exposure time: 11.9 sec. / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 50.0 µm / Calibrated magnification: 103896 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.1 µm / Nominal magnification: 59000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |