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Open data
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Basic information
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Title | E. coli ATP synthase imaged in 10mM MgATP State1 "half-up | |||||||||
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![]() | Energy / ATP hyrolysis / ATP synthesis / Motor / Membrane protein / cryoEM | |||||||||
Function / homology | ![]() proton motive force-driven plasma membrane ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / 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 / hydrolase activity / lipid binding / ATP hydrolysis activity / ATP binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||
![]() | Sobti M / Stewart AG | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Changes within the central stalk of E. coli FF ATP synthase observed after addition of ATP. Authors: Meghna Sobti / Yi C Zeng / James L Walshe / Simon H J Brown / Robert Ishmukhametov / Alastair G Stewart / ![]() ![]() Abstract: FF ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the F motor that is transferred to the F motor to ...FF ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the F motor that is transferred to the F motor to catalyze ATP production, with flexible F/F coupling required for efficient catalysis. FF ATP synthase can also operate in reverse, hydrolyzing ATP and pumping protons, and in bacteria this function can be regulated by an inhibitory ε subunit. Here we present cryo-EM data showing E. coli FF ATP synthase in different rotational and inhibited sub-states, observed following incubation with 10 mM MgATP. Our structures demonstrate how structural transitions within the inhibitory ε subunit induce torsional movement in the central stalk, thereby enabling its rotation within the F motor. This highlights the importance of the central rotor for flexible coupling of the F and F motors and provides further insight into the regulatory mechanism mediated by subunit ε. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 152.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 26 KB 26 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.5 KB | Display | ![]() |
Images | ![]() | 99.3 KB | ||
Filedesc metadata | ![]() | 7 KB | ||
Others | ![]() ![]() | 132.3 MB 132.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8dbpMC ![]() 8dbqC ![]() 8dbrC ![]() 8dbsC ![]() 8dbtC ![]() 8dbuC ![]() 8dbvC ![]() 8dbwC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1.079 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_27297_half_map_1.map | ||||||||||||
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Density Histograms |
-Half map: #2
File | emd_27297_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
+Entire : ATP synthase
+Supramolecule #1: ATP synthase
+Macromolecule #1: ATP synthase subunit c
+Macromolecule #2: ATP synthase subunit alpha
+Macromolecule #3: ATP synthase subunit beta
+Macromolecule #4: ATP synthase gamma chain
+Macromolecule #5: ATP synthase epsilon chain
+Macromolecule #6: ATP synthase subunit delta
+Macromolecule #7: ATP synthase subunit b
+Macromolecule #8: ATP synthase subunit a
+Macromolecule #9: ADENOSINE-5'-TRIPHOSPHATE
+Macromolecule #10: MAGNESIUM ION
+Macromolecule #11: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 48.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |