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- EMDB-10525: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-10525 | |||||||||||||||
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Title | Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase hexamer, membrane region | |||||||||||||||
![]() | Toxoplasma gondii ATP synthase hexamer, membrane region | |||||||||||||||
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Function / homology | ![]() mitochondrial respiratory chain complex III / photosynthetic electron transport in photosystem I / mitochondrial proton-transporting ATP synthase, stator stalk / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex / proton motive force-driven ATP synthesis / proton transmembrane transporter activity ...mitochondrial respiratory chain complex III / photosynthetic electron transport in photosystem I / mitochondrial proton-transporting ATP synthase, stator stalk / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / photosynthetic electron transport in photosystem II / proton motive force-driven mitochondrial ATP synthesis / chloroplast thylakoid membrane / proton-transporting ATP synthase complex, catalytic core F(1) / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||||||||
Method | ![]() ![]() | |||||||||||||||
![]() | Muhleip A / Kock Flygaard R / Amunts A | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria. Authors: Alexander Mühleip / Rasmus Kock Flygaard / Jana Ovciarikova / Alice Lacombe / Paula Fernandes / Lilach Sheiner / Alexey Amunts / ![]() ![]() Abstract: Mitochondrial ATP synthase plays a key role in inducing membrane curvature to establish cristae. In Apicomplexa causing diseases such as malaria and toxoplasmosis, an unusual cristae morphology has ...Mitochondrial ATP synthase plays a key role in inducing membrane curvature to establish cristae. In Apicomplexa causing diseases such as malaria and toxoplasmosis, an unusual cristae morphology has been observed, but its structural basis is unknown. Here, we report that the apicomplexan ATP synthase assembles into cyclic hexamers, essential to shape their distinct cristae. Cryo-EM was used to determine the structure of the hexamer, which is held together by interactions between parasite-specific subunits in the lumenal region. Overall, we identified 17 apicomplexan-specific subunits, and a minimal and nuclear-encoded subunit-a. The hexamer consists of three dimers with an extensive dimer interface that includes bound cardiolipins and the inhibitor IF. Cryo-ET and subtomogram averaging revealed that hexamers arrange into ~20-megadalton pentagonal pyramids in the curved apical membrane regions. Knockout of the linker protein ATPTG11 resulted in the loss of pentagonal pyramids with concomitant aberrantly shaped cristae. Together, this demonstrates that the unique macromolecular arrangement is critical for the maintenance of cristae morphology in Apicomplexa. | |||||||||||||||
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 | ![]() | 431.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 49.1 KB 49.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 21.3 KB | Display | ![]() |
Images | ![]() | 115.4 KB | ||
Masks | ![]() | 824 MB | ![]() | |
Others | ![]() ![]() | 664.4 MB 665.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6tmlMC ![]() 6tmgC ![]() 6tmhC ![]() 6tmiC ![]() 6tmjC ![]() 6tmkC 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 | Toxoplasma gondii ATP synthase hexamer, membrane region | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.05 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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Density Histograms |
-Half map: Halfmap 2
File | emd_10525_half_map_1.map | ||||||||||||
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Annotation | Halfmap 2 | ||||||||||||
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Density Histograms |
-Half map: Halfmap 1
File | emd_10525_half_map_2.map | ||||||||||||
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Annotation | Halfmap 1 | ||||||||||||
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Density Histograms |
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Sample components
+Entire : Toxoplasma gondii ATP synthase hexamer
+Supramolecule #1: Toxoplasma gondii ATP synthase hexamer
+Macromolecule #1: ATPTG11
+Macromolecule #2: ATPTG7
+Macromolecule #3: ATPTG14
+Macromolecule #4: ATPTG5
+Macromolecule #5: subunit k
+Macromolecule #6: subunit a
+Macromolecule #7: subunit i/j
+Macromolecule #8: ATPTG13
+Macromolecule #9: ATPTG15
+Macromolecule #10: ATPTG6
+Macromolecule #11: ATPTG3
+Macromolecule #12: ATPTG17,ATPTG17,ATPTG17
+Macromolecule #13: subunit b
+Macromolecule #14: ATPTG12
+Macromolecule #15: ATPTG10
+Macromolecule #16: subunit f
+Macromolecule #17: ATPTG8
+Macromolecule #18: ATPTG1
+Macromolecule #19: ATPTG2
+Macromolecule #20: subunit 8
+Macromolecule #21: ATPTG9
+Macromolecule #22: ATPTG4
+Macromolecule #23: ATPTG16
+Macromolecule #24: subunit d
+Macromolecule #25: Oligomycin sensitivity conferring protein (OSCP)
+Macromolecule #26: Inhibitor of F1
+Macromolecule #27: ATP synthase subunit alpha
+Macromolecule #28: ATP synthase subunit beta
+Macromolecule #29: ATP synthase subunit gamma
+Macromolecule #30: ATP synthase subunit delta
+Macromolecule #31: ATP synthase subunit epsilon
+Macromolecule #32: subunit c
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Concentration | 19 mg/mL |
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Buffer | pH: 7.5 |
Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER |
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 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Number real images: 7604 / Average electron dose: 32.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL |
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Output model | ![]() PDB-6tml: |