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- EMDB-10860: Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP sy... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-10860 | ||||||||||||
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Title | Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - F1Fo dimer | ||||||||||||
![]() | Local-resolution filtered full map of T. thermophila ATP synthase | ||||||||||||
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Function / homology | ![]() : / sulfide oxidation, using sulfide:quinone oxidoreductase / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||
Method | ![]() ![]() | ||||||||||||
![]() | Kock Flygaard R / Muhleip A / Amunts A | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization. Authors: Rasmus Kock Flygaard / Alexander Mühleip / Victor Tobiasson / Alexey Amunts / ![]() Abstract: Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we ...Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP synthase in its dimeric and tetrameric form. The cryo-EM structure of a ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a substoichiometrically bound ATPTT2, 40 lipids, and co-factors NAD and CoQ. A single copy of subunit ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF. Type III specific linker proteins stably tie the ATP synthase monomers in parallel to each other. The intricate dimer architecture is scaffolded by an extended subunit-a that provides a template for both intra- and inter-dimer interactions. The latter results in the formation of tetramer assemblies, the membrane part of which we determined to 3.1 Å resolution. The structure of the type III ATP synthase tetramer and its associated lipids suggests that it is the intact unit propagating the membrane curvature. | ||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 473.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 45.5 KB 45.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 21.1 KB | Display | ![]() |
Images | ![]() | 81.6 KB | ||
Masks | ![]() | 824 MB | ![]() | |
Others | ![]() ![]() | 673.3 MB 670.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6ynyMC ![]() 6ynvC ![]() 6ynwC ![]() 6ynxC ![]() 6ynzC ![]() 6yo0C M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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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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Annotation | Local-resolution filtered full map of T. thermophila ATP synthase | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: Half-map 1
File | emd_10860_half_map_1.map | ||||||||||||
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Annotation | Half-map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half-map 2
File | emd_10860_half_map_2.map | ||||||||||||
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Annotation | Half-map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
+Entire : Mitochondrial ATP synthase, F1Fo dimer
+Supramolecule #1: Mitochondrial ATP synthase, F1Fo dimer
+Macromolecule #1: subunit a
+Macromolecule #2: subunit b
+Macromolecule #3: subunit d
+Macromolecule #4: subunit f
+Macromolecule #5: subunit i/j
+Macromolecule #6: subunit k
+Macromolecule #7: subunit 8
+Macromolecule #8: ATPTT3
+Macromolecule #9: ATPTT4
+Macromolecule #10: ATPTT5
+Macromolecule #11: ATPTT6
+Macromolecule #12: ATPTT7
+Macromolecule #13: ATPTT8
+Macromolecule #14: ATPTT9
+Macromolecule #15: ATPTT10
+Macromolecule #16: ATPTT11
+Macromolecule #17: ATPTT12
+Macromolecule #18: ATPTT13
+Macromolecule #19: ATPTT1
+Macromolecule #20: Inhibitor of F1 (IF1)
+Macromolecule #21: ATPTT2
+Macromolecule #22: Oligomycin sensitivity-conferring protein (OSCP)
+Macromolecule #23: subunit gamma
+Macromolecule #24: subunit alpha
+Macromolecule #25: subunit beta
+Macromolecule #26: subunit c
+Macromolecule #27: subunit delta
+Macromolecule #28: subunit epsilon
+Macromolecule #29: CARDIOLIPIN
+Macromolecule #30: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
+Macromolecule #31: PHOSPHATE ION
+Macromolecule #32: Ubiquinone-8
+Macromolecule #33: ADENOSINE-5'-TRIPHOSPHATE
+Macromolecule #34: MAGNESIUM ION
+Macromolecule #35: 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine
+Macromolecule #36: NICOTINAMIDE-ADENINE-DINUCLEOTIDE
+Macromolecule #37: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Concentration | 0.75 mg/mL |
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Buffer | pH: 7.5 |
Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 |
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Specialist optics | Energy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Average electron dose: 30.9 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |