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- EMDB-15566: rotational state 1d of the Trypanosoma brucei mitochondrial ATP s... -
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Basic information
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Title | rotational state 1d of the Trypanosoma brucei mitochondrial ATP synthase dimer | |||||||||
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Function / homology | ![]() H+-transporting two-sector ATPase / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances / kinetoplast / ATP biosynthetic process / nuclear lumen / ciliary plasm / : / : / : / : ...H+-transporting two-sector ATPase / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances / kinetoplast / ATP biosynthetic process / nuclear lumen / ciliary plasm / : / : / : / : / proton-transporting ATP synthase complex, coupling factor F(o) / : / proton motive force-driven ATP synthesis / chloroplast thylakoid membrane / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton transmembrane transport / proton-transporting ATP synthase activity, rotational mechanism / mitochondrial membrane / ADP binding / mitochondrial inner membrane / hydrolase activity / lipid binding / ATP hydrolysis activity / mitochondrion / nucleoplasm / ATP binding / membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
![]() | Muehleip A / Gahura O / Zikova A / Amunts A | |||||||||
Funding support | European Union, 1 items
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![]() | ![]() Title: An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases. Authors: Ondřej Gahura / Alexander Mühleip / Carolina Hierro-Yap / Brian Panicucci / Minal Jain / David Hollaus / Martina Slapničková / Alena Zíková / Alexey Amunts / ![]() ![]() Abstract: Mitochondrial ATP synthase forms stable dimers arranged into oligomeric assemblies that generate the inner-membrane curvature essential for efficient energy conversion. Here, we report cryo-EM ...Mitochondrial ATP synthase forms stable dimers arranged into oligomeric assemblies that generate the inner-membrane curvature essential for efficient energy conversion. Here, we report cryo-EM structures of the intact ATP synthase dimer from Trypanosoma brucei in ten different rotational states. The model consists of 25 subunits, including nine lineage-specific, as well as 36 lipids. The rotary mechanism is influenced by the divergent peripheral stalk, conferring a greater conformational flexibility. Proton transfer in the lumenal half-channel occurs via a chain of five ordered water molecules. The dimerization interface is formed by subunit-g that is critical for interactions but not for the catalytic activity. Although overall dimer architecture varies among eukaryotes, we find that subunit-g together with subunit-e form an ancestral oligomerization motif, which is shared between the trypanosomal and mammalian lineages. Therefore, our data defines the subunit-g/e module as a structural component determining ATP synthase oligomeric assemblies. | |||||||||
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 380.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 41.3 KB 41.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 19.9 KB | Display | ![]() |
Images | ![]() | 84 KB | ||
Masks | ![]() | 669.9 MB | ![]() | |
Others | ![]() ![]() | 544 MB 544.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8apdMC ![]() 8ap6C ![]() 8ap7C ![]() 8ap8C ![]() 8ap9C ![]() 8apaC ![]() 8apbC ![]() 8apcC ![]() 8apeC ![]() 8apfC ![]() 8apgC ![]() 8aphC ![]() 8apjC ![]() 8apkC M: atomic model generated by this map C: citing same article ( |
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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: 0.83 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Half map: #1
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Density Histograms |
-Half map: #2
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Sample components
+Entire : mitochondrial ATP synthase dimer from Trypanosoma brucei
+Supramolecule #1: mitochondrial ATP synthase dimer from Trypanosoma brucei
+Macromolecule #1: subunit-e
+Macromolecule #2: subunit-g
+Macromolecule #3: ATP synthase subunit a
+Macromolecule #4: subunit-8
+Macromolecule #5: subunit-d
+Macromolecule #6: ATPTB1
+Macromolecule #7: subunit-f
+Macromolecule #8: ATPTB3
+Macromolecule #9: ATPTB4
+Macromolecule #10: subunit-i/j
+Macromolecule #11: ATPTB6
+Macromolecule #12: subunit-k
+Macromolecule #13: ATPTB11
+Macromolecule #14: ATPTB12
+Macromolecule #15: subunit-b
+Macromolecule #16: ATPEG3
+Macromolecule #17: ATPEG4
+Macromolecule #18: ATP synthase subunit alpha, mitochondrial
+Macromolecule #19: ATP synthase subunit beta, mitochondrial
+Macromolecule #20: ATP synthase gamma subunit
+Macromolecule #21: ATP synthase, epsilon chain, putative
+Macromolecule #22: ATP synthase subunit epsilon, mitochondrial
+Macromolecule #23: ATP synthase subunit p18, mitochondrial
+Macromolecule #24: OSCP
+Macromolecule #25: ATPase subunit 9, putative
+Macromolecule #26: CARDIOLIPIN
+Macromolecule #27: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
+Macromolecule #28: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
+Macromolecule #29: DODECYL-BETA-D-MALTOSIDE
+Macromolecule #30: 2-{[(4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranosyl)oxy]methyl...
+Macromolecule #31: ADENOSINE-5'-TRIPHOSPHATE
+Macromolecule #32: MAGNESIUM ION
+Macromolecule #33: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #34: URIDINE 5'-TRIPHOSPHATE
-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: 8 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Temperature | Min: 70.0 K / Max: 70.0 K |
Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Average electron dose: 33.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.2 µm / Nominal defocus min: 1.6 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |