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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | IF1 bound bovine F-ATP synthase planar dimer | |||||||||
Map data | IF1 bound planar dimer of bovine F-ATP synthase. | |||||||||
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Keywords | ATP synthase/hydrolase / oligomer / membrane bending / mammalian mitochondria / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationnegative regulation of mitochondrial ATP synthesis coupled proton transport / angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / Mitochondrial translation termination / proton channel activity / negative regulation of hydrolase activity ...negative regulation of mitochondrial ATP synthesis coupled proton transport / angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / Mitochondrial translation termination / proton channel activity / negative regulation of hydrolase activity / Mitochondrial protein degradation / negative regulation of endothelial cell proliferation / heme biosynthetic process / proton transmembrane transporter activity / proton motive force-driven ATP synthesis / proton-transporting two-sector ATPase complex, proton-transporting domain / proton motive force-driven mitochondrial ATP synthesis / MHC class I protein binding / positive regulation of blood vessel endothelial cell migration / H+-transporting two-sector ATPase / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism / proton transmembrane transport / erythrocyte differentiation / aerobic respiration / ADP binding / mitochondrial membrane / ATPase binding / protein homotetramerization / calmodulin binding / mitochondrial inner membrane / lipid binding / structural molecule activity / cell surface / protein homodimerization activity / ATP hydrolysis activity / protein-containing complex / mitochondrion / ATP binding / metal ion binding / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 5.0 Å | |||||||||
Authors | Nakano A / Jiko C / Yamashita E / Yokoyama K / Gerle C | |||||||||
| Funding support | Japan, 2 items
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Citation | Journal: Cell Death Differ / Year: 2026Title: A planar dimer of bovine ATP synthase. Authors: Chimari Jiko / Atsuki Nakano / Yosuke Teshirogi / Eiki Yamashita / Genji Kurisu / Daron Standley / Tohru Terada / Kaoru Mitsuoka / Ken Yokoyama / Christoph Gerle / ![]() Abstract: Mammalian mitochondrial ATP synthase typically organizes into rows of V-shaped dimers that impose significant membrane curvature essential for mitochondrial cristae formation. Using gentle, column- ...Mammalian mitochondrial ATP synthase typically organizes into rows of V-shaped dimers that impose significant membrane curvature essential for mitochondrial cristae formation. Using gentle, column-free purification combined with single-particle cryo-electron microscopy, we have identified a previously unrecognized planar dimeric form of bovine ATP synthase exhibiting minimal membrane bending. This planar dimer is characterized structurally by anti-parallel arrangement of two ATP synthase complexes linked by a straight conformation of inhibitory factor 1 (IF1), a sharp contrast to the kinked IF1 observed in tetrameric assemblies. Molecular dynamics simulations confirm that transitioning between straight and kinked IF1 conformations occurs without significant energetic barriers. The planar dimer also displays distinct peripheral stalk positioning relative to its adjacent α subunit. These structural divergences suggest a specialized function and a distinct localization for planar ATP synthase dimers, providing structural support for a division of labor within mitochondrial ATP synthase populations. #1: Journal: Biorxiv / Year: 2025Title: A planar dimer of bovine ATP synthase Authors: Jiko C / Nakano A / Teshirogi Y / Yamashita E / Kurisu G / Standley D / Terada T / Mitsuoka K / Yokoyama K / Gerle C | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_65237.map.gz | 30.2 MB | EMDB map data format | |
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| Header (meta data) | emd-65237-v30.xml emd-65237.xml | 37.2 KB 37.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_65237_fsc.xml | 8.2 KB | Display | FSC data file |
| Images | emd_65237.png | 130.5 KB | ||
| Masks | emd_65237_msk_1.map | 59.6 MB | Mask map | |
| Filedesc metadata | emd-65237.cif.gz | 9.1 KB | ||
| Others | emd_65237_half_map_1.map.gz emd_65237_half_map_2.map.gz | 55.3 MB 55.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-65237 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-65237 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9vpbMC ![]() 9vpcC ![]() 9vpdC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_65237.map.gz / Format: CCP4 / Size: 59.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | IF1 bound planar dimer of bovine F-ATP synthase. | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 2.184 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_65237_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: half map B
| File | emd_65237_half_map_1.map | ||||||||||||
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| Annotation | half map B | ||||||||||||
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| Density Histograms |
-Half map: half map A
| File | emd_65237_half_map_2.map | ||||||||||||
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| Annotation | half map A | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Bovine F-ATP synthase in the oligomeric form of an IF1 bound plan...
+Supramolecule #1: Bovine F-ATP synthase in the oligomeric form of an IF1 bound plan...
+Macromolecule #1: ATP synthase F(0) complex subunit 8
+Macromolecule #2: ATP synthase subunit alpha
+Macromolecule #3: ATP synthase F(1) complex catalytic subunit beta, mitochondrial
+Macromolecule #4: ATP synthase F(1) complex subunit gamma, mitochondrial
+Macromolecule #5: ATP synthase F(1) complex subunit delta, mitochondrial
+Macromolecule #6: ATP synthase F(1) complex subunit epsilon, mitochondrial
+Macromolecule #7: ATPase inhibitor, mitochondrial
+Macromolecule #8: ATP synthase F(0) complex subunit C2, mitochondrial
+Macromolecule #9: ATP synthase peripheral stalk subunit OSCP, mitochondrial
+Macromolecule #10: ATP synthase F(0) complex subunit a
+Macromolecule #11: ATP synthase peripheral stalk subunit b, mitochondrial
+Macromolecule #12: ATP synthase peripheral stalk subunit d, mitochondrial
+Macromolecule #13: ATP synthase F(0) complex subunit e, mitochondrial
+Macromolecule #14: ATP synthase F(0) complex subunit f, mitochondrial
+Macromolecule #15: ATP synthase F(0) complex subunit g, mitochondrial
+Macromolecule #16: ATP synthase peripheral stalk subunit F6, mitochondrial
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 5 mg/mL |
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| Buffer | pH: 7.3 |
| Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 2 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
Japan, 2 items
Citation

















Z (Sec.)
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Processing
FIELD EMISSION GUN



